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IEJ/T^ ~7NQoB0njkCRG)4<5 /;#p(5UU+C[!sjti%QcS[qY}ÿeRYnz>74'TEsT9[T)jImF5o;\+77N+s¶]g[[\(&V4E* 7v鬭8 YB&)6=,pȦ.J5'J\m=+u d2*yED%GL7n2b2d1|Ý\-kDHINN-6LOCo,{XgM~s<[PK!ކAdrs/downrev.xmlLN1E&CLI (B1$|3}0 ޜ3[e'A;+a8VNi[K|=LVa,IPfrg:,AlPBcq ȦnxNpnP`GyCqc$r3|(?ów H}G~(?T$ RzV"y /&S_PK-!Zf[Content_Types].xmlPK-!1_a /_rels/.relsPK-!R*drs/shapexml.xmlPK-!ކAdrs/downrev.xmlPKAWB:2___PPT9  T   z \ RA??Picture 5s z \ RA??Picture 6  z \ RA??Picture 7V   \ X Ԕ?Text Box 8"PK![Content_Types].xml|N0 HC+jS8 @:Q۸ ??\o<7p]V޷O(I'6E=, ){Ō4>I)q7UuDހǏ)}nL"Mᴸ&g0eSA)΄2';2 WYu7{ɯΒzŘqFrj9K*(]mOlPK!Z,[ _rels/.relslj0 ``t_Pƈ[>,dgzjǎ?I'f#®Pb-\/Ƿ0Z]nLnp__3.iJV KQBiDžrL,Vʌ/7р4`ANar+m;E/'3U Aںv83/PK! Vvdrs/downrev.xmlDn0V8(B#B+.Dבm kWO3_gua<@Wδ\kX=LAlsL`ca܅K:oc-CBP5d1\Oy1%m'Ubi^'O~<ƽZjVXf " YmuUo&1W[Sb5ԛ8PK-![Content_Types].xmlPK-!Z,[ _rels/.relsPK-! Vvdrs/downrev.xmlPK H ,$D nPROVED CORRECT (   G[۴Pܝ7___PPT10.ofoc+P!wDO' = @B D ' = @BA?%,( < +O%,( < +DA' =%(D' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<* \%(+8+0+ \ +" [+  JB`*(  `2 `  x 0e0e ?Rectangle 2F  d fThe SPiM Simulator&    `  x  ?Rectangle 3 d wSimulation algorithm mapped to functional code (F#) Used as the basis for implementing the SPiM simulator. [Phillips, 2006] GUI by James Margetson, MSRC Close correspondence between formal algorithm and functional code Correct specification improves confidence in simulation results Used in various research centres (UK, France, Italy, Sweden, Canada, Philippines, Japan,...).4 D 4D>  7 @` ` fP ?6Slide Number Placeholder 4   l*    ` jA  ?? SPiMPicture 4SPiM"@@ Z_ ` LQ ?Text Box 5:! ,http://research.microsoft.com/~aphillip/spim- - -  G[۴Pܝ7___PPT10i.o]+D=' = @B +" (+  0 d(  d+ d  xR 0e0e ?Rectangle 2F  d _Visualising Simulations in 3D   d  ~S  ?Rectangle 3 d GGenerate a 3D view of the interactions Software by Rich Williams, MSRC,' ! '! 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mapkPicture 13mapk6  G[۴Pܝ7zr___PPT10R.>O+ leD&' = @B D`' = @BA?%,( < +O%,( < +D' =%(%(D' =%(D=' =4@BBBB%(D'  =2y;BplayFrom(0.0)*<3<*dD=' =4@BBBB%(D' (=2y;BplayFrom(0.0)*<3<* dD=' =4@BBBB%(D' ,=2y;BplayFrom(0.0)*<3<* dD'  =0BcancelBubble@BA?%<(<*d%<(<*d_%(D' =%(D' =%(D9' =4@BBBB%(D' =2u;BtogglePause*<3<*dD'  = B`B?<*d%(/%,( < +/%,( < +)D'  =0BcancelBubble@BA?%<(<* d%<(<* d_%(D' =%(D' =%(D9' =4@BBBB%(D' =2u;BtogglePause*<3<* dD'  = B`B?<* d%(/%,( < +/%,( < +)D'  = B`B?<* d%(/%,( < +/%,( < +)D'  =0BcancelBubble@BA?%<(<* d%<(<* d_%(D' =%(D' =%(D9' =4@BBBB%(D' =2u;BtogglePause*<3<* d+" Ph(  h7 h  x\ 0e0e$?Rectangle 2 dp k'Introduction to Stochastic Pi-calculus( (( (D h  x 0e0e$?Rectangle 3   dp xChemical Reactions(   @` G[۴Pܝ7___PPT10i.P;Z+D=' = @B + + pl(  l l  x\ 0e0e ?Rectangle 3F  d BIonization: Na + Cl Na+ + Cl-x" CCKCK " l  x`  ?Rectangle 2  d Z Na can ionize Cl at rate(ionize) = 100s-1 Cl- can deionize Na+ at rate(deionize) = 10s-1.[          [ @` l f ?6Slide Number Placeholder 4   l*    l jA* ?? naclPicture 4nacl t V l H ?Rectangle 5   Flet Na() = !ionize; Na_plus() and Na_plus() = ?deionize; Na() run Na()$G~0 PZG: h, l H ?Rectangle 6p ` Hlet Cl() = ?ionize; Cl_minus() and Cl_minus() = !deionize; Cl() run Cl()$I~0 PZII h G[۴Pܝ7___PPT10i.L+D=' = @B +"u + aY pA(  p p  x 0e0e ?Rectangle 2F  d BIonization: Na + Cl Na+ + Cl-x" CCKCK " p  x  ?Rectangle 3  d 3Na can ionize Cl by an output on the ionize channelN4   4 @` p f ?6Slide Number Placeholder 4   l*    p jA* ?? naclPicture 4nacl t .  p `@ ?Rectangle 5"PK!Zf[Content_Types].xmlMO &2WR=cJ`F0iK`#̼vLw 9uSq:w`G ^i ½KI)c/ $oVjTMRc|}042ҥCƔM̏P~*ka/8^DkHbL8e i"K\XN\6rco4y@_;oPK!1_a _rels/.relsj0 ѽqCNo^K [ILcX&m߾0XFo;>0xM e`|X}đ I`߽N4aG2$RKIZ)4(M9`ctB{m:f@`3n|O,ܗr޾jxR0T ,0@}WBLǬ5vPK!cN_Rdrs/shapexml.xmlUn0 }:tq.%;ò=dEt@rE IΥ_?RraYRʢC}VZW3)*5g΃.@-3~}C3u MokY{oq4K4V:=x T(I.5TUzl,]XV*]pR ,3D27b:87p ;$LOk!5! 65BOg)+`^0ݗ>cʒ퉒(2> r d2IRzM y6/ҜEX)l)UJl *I2avT5M/T cGAJ2~^J0ԡLUuƯ IWjϺ.*mJi#iD΅E\Q{S(@=x,k@T/(3Vʚ&;^d<Cmy8trLP+>Y!'ȗXdcGo s}o7$4߅#98Bn,Z-ah L c pk߾qڽ+ݼőyZvܛ3L_<`Q xBPR ٦"sƥr7 ;y[mP$Yuj1*Y~ K"]U6 kLI6d?axd/$~%XTCI \/Ŏ媵-S U+mU@J6/k2~]}dXvAC#Kӝ[:Z>Z wGYWuNJ3AznPK!]drs/downrev.xmlD1O0Fw$uHlԡ uĀv(_c؎lM=wz|9Il뤶Xh%Β X.XJw ֱcIbCTCyh 7MlNq,˹AmӂX C}qWlSBތHcWUԒ|lzZ6"y0&|PK-!Zf[Content_Types].xmlPK-!1_a /_rels/.relsPK-!cN_R*drs/shapexml.xmlPK-!]drs/downrev.xmlPK,n$@:2___PPT9  P   1  p `` ?Rectangle 6"PK!Zf[Content_Types].xmlMO &2WR=cJ`F0iK`#̼vLw 9uSq:w`G ^i ½KI)c/ $oVjTMRc|}042ҥCƔM̏P~*ka/8^DkHbL8e i"K\XN\6rco4y@_;oPK!1_a _rels/.relsj0 ѽqCNo^K [ILcX&m߾0XFo;>0xM e`|X}đ I`߽N4aG2$RKIZ)4(M9`ctB{m:f@`3n|O,ܗr޾jxR0T ,0@}WBLǬ5vPK!icRdrs/shapexml.xmlUn8}/@uZ\(ARo`("%_R`Q, d(9g=kͶyeM·3ΤTfﯳ|SF =]3 OChkYlipK4Nzi T(ˮ5(*]6 Gx.S%bH0VZ+>Y)W(oX%V%͓ېʚ fmRONbǡmqr ݺiJJE2/p"͊R[}ЮA7Ӯp|/J֋n+aKٱ!Y84<=:b Y i!|TQo:PK!drs/downrev.xmlDN0 @HCd$n,e+eS(0u7xMYTIuOH>tN2č ޷7 BD;&g \\^̱57I¡@&ơ24,9o1ѷR{<%4fb 5*XUo5r60a[J]_#Hc?௪ҩeMԳ{9N"yizPK-!Zf[Content_Types].xmlPK-!1_a /_rels/.relsPK-!icR*drs/shapexml.xmlPK-!drs/downrev.xmlPK, n$D:2___PPT9  P   V p H ?Rectangle 8   Flet Na() = !ionize; Na_plus() and Na_plus() = ?deionize; Na() run Na()$G~0 PZG: h,  p H ?Rectangle 9p ` Hlet Cl() = ?ionize; Cl_minus() and Cl_minus() = !deionize; Cl() run Cl()$I~0 PZII h G[۴Pܝ7___PPT10.L+,gD' = @B D' = @BA?%,( < +O%,( < +D' =%(D' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*p%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*p%(+p+0+p ++0+p +" +  t(  t t  x 0e0e ?Rectangle 2F  d BIonization: Na + Cl Na+ + Cl-x" CCKCK " t  x  ?Rectangle 3  d 9Cl- can deionize Na+ by an output on the deionize channelt:      : @` t f ?6Slide Number Placeholder 4   l*    t jA+ ?? naclPicture 4nacl t 4  t ` ?Rectangle 5"PK!Zf[Content_Types].xmlMO &2WR=cJ`F0iK`#̼vLw 9uSq:w`G ^i ½KI)c/ $oVjTMRc|}042ҥCƔM̏P~*ka/8^DkHbL8e i"K\XN\6rco4y@_;oPK!1_a _rels/.relsj0 ѽqCNo^K [ILcX&m߾0XFo;>0xM e`|X}đ I`߽N4aG2$RKIZ)4(M9`ctB{m:f@`3n|O,ܗr޾jxR0T ,0@}WBLǬ5vPK!2eRdrs/shapexml.xmlUn8}/@uZ86In0([kHʗ|}gHYNE7PrΜ9{8ԊuO?'I-LQuƿίn9sthtOw5 k7k2 Nld iƽ<.zX1P$Pi~WݪYZniYU p:LC_@k%٘:xˆSXc?!a|` ho$aPAv¨bx?B CiKQ=,!t2svh4LqB`& tHGt"g=xADBu4btQ-V%d D9sFUżR`uEY$1; @:N/T cGAJ_3>c%:m(P2U%$]yEpPh#UJ,FRX?e%x2ő3NF qmlAqjwH脳Ǔ,?=݈c-!КޜcڵgfK%X̶m]*9g\ꫯO\ ^sERU8JKo> (\CIM䷰$UEokƔd8O@GJBQ߉UH40-jSYZ0xM e`|X}đ I`߽N4aG2$RKIZ)4(M9`ctB{m:f@`3n|O,ܗr޾jxR0T ,0@}WBLǬ5vPK!]eRdrs/shapexml.xmlUn8}_`"$NlT)b}F~l)R )_!e9 Ţ<8Cq9sfc^ZWC™”3A9?I?=vZ9zG#'R^elv3jtR{Q,Ij*_+K_YVez7fih0c$Q"Ys=/pJ $L[!5! 6 5B/goS"V`~ls-*T;|β1V8KIB`. tHtf , <[iF袜[JK牔K 猪EⳲl*IX`vTu_ƎӀ ;|6&!6`CS{izKX'#9`1)! 5MxeiקE^0V:$COXE#r u0ưE۳ sd9 ]BI]~fOIŜs.͗'|.,WDowmCf,vۃO ץŐpR+WWX骦ݵYYc* _a a#%!(o*zJZz-P}|X?ldpXDdw,W; @7Ѯq:%ĂNwKݗ# А̟ZY@m b  q{!\RAo:;PK!BW%drs/downrev.xmlD1O0Fw$uHlԡB uĀv(_c؎lM=wz|9Il뤶Xh%Β X.XJw ֱcIbCTCyh 7MlNq,˹AmӂX C}qWlSBތHcWUԒtlzZ6"y0&|PK-!Zf[Content_Types].xmlPK-!1_a /_rels/.relsPK-!]eR*drs/shapexml.xmlPK-!BW%drs/downrev.xmlPK,=n$D:2___PPT9  P   [ t Hঢ় ?Rectangle 7   Klet Na() = !ionize; Na_plus() and Na_plus() = ?deionize; Na() run Na_plus()$L~0 PZL:h2  t H ?Rectangle 8p ` Nlet Cl() = ?ionize; Cl_minus() and Cl_minus() = !deionize; Cl() run Cl_minus()$O~0 PZOO h G[۴Pܝ7___PPT10.L+,gD' = @B D' = @BA?%,( < +O%,( < +D' =%(D' =%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*t%(D' =A@BBBB0B%(D' =1:Bvisible*o3>+B#style.visibility<*t%(+p+0+t ++0+t +"+ x(  x x  x 0e0e ?Rectangle 2F  d BIonization: Na + Cl Na+ + Cl-x" CCKCK "m x  x@  ?Rectangle 3  d Na and Cl are no longer charged8   @` x f@ ?6Slide Number Placeholder 4   l*    x jA* ?? 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Y2+D=' = @B +"+.  (  '   x 0e0e ?Rectangle 2F  d [Repressilator with Dimers     ~  ?Rectangle 6  d Refined model of a gene with cooperative binding Different implementation, same main program Neg(lac,tet) | Neg(tet,lambda) | Neg(lambda,lac)   @`   ~  ?Rectangle 3q  d  let Neg(a:chan,b:chan) = ( new b2@dimerize:chan Neg2(a,b2,b) ) and Neg2(a:chan,b2:chan,b:chan) = do delay@transcribe; (Protein(b2,b) | Neg2(a,b2,b)) or ?a; Blocked(a,b2,b) and Blocked(a:chan,b2:chan,b:chan) = delay@unblock; Neg2(a,b2,b) and Protein(b2:chan, b:chan) = do ?b2; Protein2(b) or !b2 or delay@degrade and Protein2(b:chan) = do !b; Protein2(b) or delay@degrade4  P F   @`  fV ?6Slide Number Placeholder 4   l*     jA> ?? Neg2Picture 7Neg2 [ G[۴Pܝ7___PPT10i. c@+D=' = @B +"+/  vnV(  '   x 0e0e ?Rectangle 2F  d [Dimers Improve Regularity     ~   ?Rectangle 3 d Proteins form dimers first Improves regularity of oscillations Investigating stochasticity, cooperativity, ODEs [Blossey, Cardelli, Phillips, 2007] P  @`  f! ?6Slide Number Placeholder 3   l*   z  RA???Picture 4``? z  RA@??Picture 6 lFh  G[۴Pܝ7___PPT10i. c+D=' = @B +"+0  (  >   x@% 0e0e ?Rectangle 2F  d r(Bacteria Logic Gates [Guet et al., 2002]) )V   x  ?Rectangle 3b  d 3 genes: tetR, lacI, lcI 5 promoters: PL1, PL2, PT, Pl-, Pl+ 125 possible networks consisting of 3 promoter-gene units 2 inputs: IPTG (represses Lac), aTc (represses Tet) 1 output: GFP (linked to Pl-)tCCCC  @`  f' ?6Slide Number Placeholder 4   l*   z  RAA??Picture 4A .:   F) ?Text Box 5" PK!Zf[Content_Types].xmlMO &2WR=cJ`F0iK`#̼vLw 9uSq:w`G ^i ½KI)c/ $oVjTMRc|}042ҥCƔM̏P~*ka/8^DkHbL8e i"K\XN\6rco4y@_;oPK!1_a _rels/.relsj0 ѽqCNo^K [ILcX&m߾0XFo;>0xM e`|X}đ I`߽N4aG2$RKIZ)4(M9`ctB{m:f@`3n|O,ܗr޾jxR0T ,0@}WBLǬ5vPK!  drs/shapexml.xmlVMo8/uJ5IbDQ6)?;C*6(FH(~ 9oo|{5I59> 9FRuοf|SF(=f69߄L/66Ze] n=hփzP22epOcc6Fjt큍3,pq)Vl} ~U`~if-ғ;^D&O=*AClv\}.* Vh'luft]6R.O&! 4]_D0%d8>K{6&FIb@)9 wΔ& ƨ͹ǰ}?/pBOUiUcmh@| 'B#E[IJIH'4S]J}X:QVYP5yΑwyLר3RV+(/xhDtu!YKGc5!n)K4q )5O*Ͳ)}b!Wd(7PuEI!h/}wa'ҎOEb6``붭UmS)qՌPI9+Rcܠ mC.ctqΰq!ErHу gmE}BGl +Lժr٢ρĜKodU`&hm r ݺgo Hk#mKȼ[hn6^;B{LB/wڼ&k0z&M1O,ΤEӠ썣4o*M(~:s$Νխ; PK!(drs/downrev.xmlDAO1&fHI+Aİ}nVX==N{{۲#h0 `*k$?^nńNaI8Sj'c!.(AJ8>XL WOn[~'=h\nѳz޷^Mgof/%s\?_zUƏI_o·`c !el |vPK-!Zf[Content_Types].xmlPK-!1_a /_rels/.relsPK-!  *drs/shapexml.xmlPK-!(drs/downrev.xmlPK't,B:2___PPT9   2002 AAAS. Reprinted with permission from Guet et al. Combinatorial Synthesis of Genetic Networks. 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Long-term benefits for medical research: Better understand disease. Speed up the design of a cure. Long-term benefits for computing: Write more robust concurrent / distributed programs Design and verify biological computers Smart drugs? Computers in a test tube...? Biological modelling is pushing the boundaries of concurrent programmingP P* P) P; P" P PI PP*);"I @`  f~ ?6Slide Number Placeholder 3   l*    G[۴Pܝ7y___PPT10Y+D=' = @B +"+PiJZ  (     x0 0e0e ?Rectangle 2F  d IThanks.  .   ~ 1  ?Rectangle 3 d \   @`  f@2 ?6Slide Number Placeholder 3   l*    G[۴Pܝ7___PPT10i.4 W+D=' = @B +"+LZ u m @ U (     x`3 0e0e ?Rectangle 2F  d L References       ~4  ?Rectangle 3 d   [Blossey et al., 2006] Blossey, R., Cardelli, L., and Phillips, A. (2006). A compositional approach to the stochastic dynamics of gene networks. Transactions in Computational Systems Biology, 3939:99 122. [Gillespie, 1977] Gillespie, D. T. (1977). Exact stochastic simulation of coupled chemical reactions. J. Phys. Chem., 81(25):2340 2361. [Guet et al., 2002] Guet, C.C., Elowitz, M.B., Hsing, W. & Leibler, S. (2002) Combinatorial synthesis of genetic networks. Science 296 1466-1470. [Huang and Ferrel, 1996] Huang, C.-Y. F. and Ferrel, J. E. (1996). Ultrasensitivity of the mitogen-activated protein kinase cascade. PNAS, 93:10078 10083. [Lecca and Priami, 2003] Lecca, P. and Priami, C. (2003). Cell cycle control in eukaryotes: a biospi model. In BioConcur 03. ENTCS. [Phillips, 2006] Phillips, A. (2006). The Stochastic Pi-Machine: A Simulator for the Stochastic Pi-calculus. Available from http://research.microsoft.com/aphillip/spim/. [Phillips and Cardelli, 2004] Phillips, A. and Cardelli, L. (2004). A correct abstract machine for the stochastic pi-calculus. In Bioconcur 04. ENTCS. [Phillips and Cardelli, 2005] Phillips, A. and Cardelli, L. (2005). A graphical representation for the stochastic pi-calculus. In Bioconcur 05. d  @`  f5 ?6Slide Number Placeholder 3   l*    G[۴Pܝ7___PPT10i.md`_i<+D=' = @B +"+MZ   P  (     x6 0e0e ?Rectangle 2F  d L References   N    ~7  ?Rectangle 3 d |  [Phillips et al., 2006] Phillips, A., Cardelli, L., and Castagna, G. (2006). A graphical representation for biological processes in the stochastic pi-calculus. Transactions in Computational Systems Biology, 4230:123 152. [Priami, 1995] Priami, C. (1995). Stochastic p-calculus. The Computer Journal, 38(6):578 589. Proceedings of PAPM 95. [Priami et al., 2001] Priami, C., Regev, A., Shapiro, E., and Silverman, W. (2001). Application of a stochastic name-passing calculus to representation and simulation of molecular processes. Information Processing Letters, 80:25 31. [Regev et al., 2001] Regev, A., Silverman, W., and Shapiro, E. (2001). Representation and simulation of biochemical processes using the pi- calculus process algebra. In Altman, R. B., Dunker, A. K., Hunter, L., and Klein, T. E., editors, Pacific Symposium on Biocomputing, volume 6, pages 459 470, Singapore. World Scientific Press. [Sangiorgi and Walker, 2001] Sangiorgi, D. and Walker, D. (2001). The -calculus: a Theory of Mobile Processes. Cambridge University Press. [Silverman et al., 1987] Silverman, W., Hirsch, M., Houri, A., and Shapiro, E. (1987). The logix system user manual, version 1.21. In Shapiro, E., editor, Concurrent Prolog: Collected Papers (Volume II), pages 46 77. MIT Press, London. 0 d C  @`  f ?6Slide Number Placeholder 3   l*    G[۴Pܝ7___PPT10i.md@m+D=' = @B +"   0j(    f y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZPP  d_   ~  y˼y˼?Rectangle 3]C  d C [Intro] This talk presents some ongoing work on a programming language for biological systems Most of this work was done in collaboration with Luca Cardelli [Abstract] This talk presents a programming language for designing and simulating computer models of biological systems. The language is based on a computational formalism known as the pi-calculus, and the simulation algorithm is based on standard kinetic theory of physical chemistry. The language will first be presented using a simple graphical notation, which will subsequently be used to model and simulate a number of intriguing biological systems, including a genetic oscillator and a pathway of the immune system. One of the benefits of the language is its scalability: large models of biological systems can be programmed from simple components in a modular fashion. D D D  3380___PPT10.[dqw  Po(    f y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZQQ  dd   ~ y˼y˼?Rectangle 3]C  d DIn many ways, biological systems are like massively parallel, highly complex, error-prone computer systems. For example, the genetic code of a biological organism is stored in digital form as DNA, much like a computer code, except that instead of 0s and 1s there are four letters, G,A,T,C. The code is located inside every cell of the organism. A special protein travels along the DNA to read the code, much like a computer reads a sequence of instructions in a program. Not all of the DNA is read at once. Instead, the DNA is divided into sections or genes, in the same way that a computer program is divided into modules. In general, each gene produces a separate strand of RNA, which is more accessible, like loading a module into memory. The RNA produces protein, which folds into different shapes to perform the essential functions of a living organism. Some proteins can decide which genes are switched on and off, and when. They do this by interacting with the DNA, in the same way that a computer program decides what code to execute next in response to signals from its environment. E EE   3380___PPT10.5) x    p (    f y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZPP  d~   ~@ y˼y˼?Rectangle 3]C  d The Human Genome Project had the ambitious goal of mapping out the complete genetic code in humans. Scientists had hoped that by discovering this code, they would be able to understand and predict the behaviour of genes and proteins in the human body. A bit like reading the source code of a computer program in order to find out what it does. Instead, what they got was a long sequence of letters that was difficult to understand. Like studying a sequence of 0s and 1s from a computer program, and trying to find out what the program does. They did not know the set of instructions that the genetic code represented. It was then that the discipline of Systems Biology emerged, whose ultimate goal is to decipher the code of the human genome, in order to understand how we function as a complex system. Systems Biology can be broadly divided into two complementary approaches. On the one hand, scientists are doing experiments in the lab and studying the results, in order to infer general properties of biological systems. On the other hand, scientists are trying to build detailed models of systems on a computer and then testing these models in the lab. This is the approach that we are focussing on. Such models can be a powerful tool, since they allow a biologist to simulate a range of experiments on a computer, before testing the most promising ones in the lab, saving considerable time and money. Theyalso clarify how a biological system functions, and are beginning to play a key role in understanding and curing disease. In order to build such models, we need tools that are suitable for modelling complex, parallel biological systems. We also need tools that can scale up to very large systems. This points towards the need for a biological programming language.  Zx# b /  0   3380___PPT10.[; L  y     (    f y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZPP  d   ~! y˼y˼?Rectangle 3]C  d Over the years, there has been considerable research on designing programming languages that are suitable for developing complex parallel computer systems. Interestingly, some of this research is also applicable to biological systems, which are typically highly complex and massively parallel. One example of such a language is the stochastic pi-calculus... Think about computer networks. Lots of things happening in parallel on different machines. They can interact. Not sure when. We don t know when a user is going to switch off a machine. Don t know when a cell is going to die. Need robustness. *** [Computing] In many ways, biological modelling is pushing the boundaries of concurrent programming. From a computer science perspective this is becomming increasingly important, as multi-core takes over to compensate for limited clock speeds. U U"   3380___PPT10.po"Nx  B:"(    f# y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZPP  d   ~@% y˼y˼?Rectangle 3]C  d QTo illustrate our approach, we can look at how biological modelling is typically done today. Most models are constructed by describing individual reactions. In this diagram, each shape represents a protein in the system, and each box represents a reaction. For example, the red protein can react with the yellow protein by doing a bind reaction. But what happens if we add a new component, say an orange protein? We need to explicitly state how it can interact with all the other proteins in the system.     33y  meM(    f& y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZPP  dB   ~@( y˼y˼?Rectangle 3]C  d |&Each time we add a new protein, we need to add lots of new reactions. This can lead to a combinatorial explosion in the number of nodes and edges in the graph. (For example, the orange protein can bind to the yellow protein in presence of the green protein, but so can the red protein, etc.)' ' '  33z  zb(    f) y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZPP  dW   ~@+ y˼y˼?Rectangle 3]C  d ;Until eventually we end up with a very large, highly connected reaction graph. But what happens if we want to change our model of a particular protein? This is difficult to do, since the model is not constructed in a modular way. We need to go through the model to find all the reactions related to that protein. < < <  3380___PPT10.f‘{  |(    f`, y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZPP  dq   ~- y˼y˼?Rectangle 3]C  d To solve this problem, instead of modelling the reactions of a biological system, we model its components. In this diagram, the behaviour of each protein is described by a separate graph. We have a graph for the red protein, one for the yellow protein, etc. Each node in the graph represents a state of the protein, and each edge represents a reaction. Instead of explicitly saying which protein interacts with which other protein, we describe the different sites on which a protein can interact. This adds a layer of abstraction to the model, where two proteins can interact with each other if they can interact on complementary sites. For example, in the graph we see that the yellow protein can interact on a particular site ?bind. We also see that the red protein can interact on a complementary site !bind (where ? and ! denote complementary sites) , and so can the orange protein. So we deduce that the yellow protein can interact with both the red and orange proteins. This approach also has a lot in common with biological reality. If we think in terms of DNA, we know that complementary DNA sequences can interact. So rather than explicitly saying which sequence interacts with which other sequence, we simply check to see which sequences are complementary.@ G s@ :G s@   33C|  0(    f0 y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZPP  d   ~? y˼y˼?Rectangle 3]C  d This allows us to build large and complex models by directly composing simpler components. It also allows us to modify a particular component in a modular way, without changing the rest of the graph. As biological models become increasingly large and complex, modular programming languages could have just as big an impact for biology as they did for computing. Consider the development of higher-level languages on top of assembly language.    33}  RJP2(    f`? y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZPP  d'   ~< y˼y˼?Rectangle 3]C  d a The pi-calculus is also a mathematical programming language, with decades of research on analysis techniques. Many of these techniques are directly applicable to biological modelling, and could help provide insight into fundamental properties of biological systems.       33~  p(    f@; y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZPP  d   ~9 y˼y˼?Rectangle 3]C  d uFor example, we can use existing tools to automatically verify: when is it safe to replace one system with another? v v v  33\w  (     0e0e?4Slide Image Placeholder 1ZPP  dw   @" y˼y˼?(Notes Placeholder 2]C  d gBriefly discuss some of the initial challenges we faced in developing a biological programming language h /  `# y˼y˼?6Slide Number Placeholder 3b   j*   a 3380___PPT10.)@a  (    f@% y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZPP  d   ~`& y˼y˼?Rectangle 3]C  d There has been considerable work on using the stochastic pi-calculus to model biological systems. We are building on this work in our current research.     3380___PPT10.oz  \T<(    f@( y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZPP  d1   ~@. y˼y˼?Rectangle 3]C  d kOne of our first projects was to develop a graphical representation for the stochastic pi-calculus, to make the calculus more accessible to biologists. We proved the equivalence between the textual and graphical representations, showing that they can be used interchangeably.     3380___PPT10.oPS)  (    f9 y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZPP  d~   ~= y˼y˼?Rectangle 3]C  d bWe also developed the first provably correct simulation algorithm for the stochastic pi-calculus. c c c  3380___PPT10.ob  ~v ^(    f@; y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZPP  dS   ~`< y˼y˼?Rectangle 3]C  d 7We used this algorithm to implement a stochastic simulator in F# The nice thing about F# is that it is very close to our formal specification. This allowed rapid implementation, and also improved our confidence in the simulation results. The simulator is now used in various research centres around the world. 8 8 8  3380___PPT10.@ N  @(    f( y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZPP  d   ~< y˼y˼?Rectangle 3]C  d We also used our graphical representation to generate a 3D view of simulations. This is particularly useful for debugging our models.     3380___PPT10.>3ٌ*  qi`Q(     0e0e?4Slide Image Placeholder 1ZPP  d     4 y˼y˼?(Notes Placeholder 2]C  d 6  /  `3 y˼y˼?6Slide Number Placeholder 3b   j*   a 3380___PPT10.E=3  (    f* y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZQQ  d   ~`, y˼y˼?Rectangle 3]C  d vLet's take something you should all be familiar with: Na + Cl -> Na+ + Cl- The code and the picture are isomorphic. The Na can ionize Cl by sending an electron on the ionize channel. Becomes positively charged. The Cl can become ionized by receiving an electron on this channel. Becomes negatively charged. Note that the behaviour of both atoms can be described independently. When they interact, they both become charged simultaneously. Think of this as a synchronisation. The rate denotes the speed of the reaction. [Ex] Type in the code for Na. Ask participants to type in the code for Cl, just by looking at the picture.w w w  3380___PPT10.5l?  rjPR(    f/ y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZPP  dG   ~` y˼y˼?Rectangle 3]C  d +[Ex] what simulation results do you expect?, , ,  3380___PPT10.q jA  jbJ(    f y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZPP  d?   ~  y˼y˼?Rectangle 3]C  d y#[ISS] Why is there an equilibrium? $ $ $  3380___PPT10.q`x(  qiQ(     0e0e?4Slide Image Placeholder 1ZPP  d    ` y˼y˼?(Notes Placeholder 2]C  d 6  /   y˼y˼?6Slide Number Placeholder 3b   j*   a 3380___PPT10.]Nu  C;#(    f` y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZPP  d   ~ y˼y˼?Rectangle 3]C  d R    3380___PPT10.[dqd  (     0e0e?4Slide Image Placeholder 1ZPP  d    y˼y˼?(Notes Placeholder 2]C  d IThis video simulates a computer model of a biological clock, which was engineered in living bacteria. The clock works by producing alternate populations of red, blue and purple proteins. These regular oscillations are used to define a notion of time. Our biological clock works using a similar principle, where a large population of a particular protein is produced every 24 hours. The nodes at the bottom represent genes, which can be in two states, on or off. The nodes at the top represent proteins, where the volume of the node is proportional to the population. The green nodes represent actions: inputs, outputs, delays. The green edges represent interactions, and go from an output to an input on the same channel. The proteins are constantly being produced and degraded. The proteins from one gene can switch off another gene. I J J /    y˼y˼?6Slide Number Placeholder 3b   j*   a 3380___PPT10.@?  ( (    f y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZPP  d   ~ y˼y˼?Rectangle 3]C  d 7The basic building block of our clock is a gene with negative control. The graphical representation on the left of the figure is equivalent to the textual representation on the right. (bottom) The gene is parameterised by two proteins, a and b. The gene produces protein b, and is blocked by protein a. (middle) Each shape in the graph represents a gene or protein in particular state, and each labelled edge represents an action that the Gene or protein can perform. Multiple edges from a species correspond to a choice, while multiple edges from a horizontal bar correspond to a parallel composition. (middle) The graph shows the dynamic behaviour of the Gene. Each node in the graph represents a separate molecule in a given state. The node shaped like a strand of DNA represents a Gene(a,b). The node shaped like a strand of DNA with a blocked promoter region represents the gene in a blocked state, called Blocked(a,b), and the node shaped like a round blob represents a Protein(b). Each labelled edge in the graph represents a reaction. There are two types of reaction: unary and binary. Unary reactions are labelled with the reaction name. For example, a protein can degrade by doing a degrade reaction. Binary reactions are labelled with the reaction channel preceded by an input (?) or output (!) prefix. For example, a Gene(a,b) can become blocked by doing an input on channel a and a Protein(b) can react by doing an output on channel b. Two molecules can interact by doing a complementary input and output on the same channel. For example, if there was a Protein(a) it could interact with the promoter region of a Gene(a,b), causing the gene to block. This interaction between complementary inputs and outputs allows us to construct networks of genes, as we shall see later on. A branching edge is used to represent the production of a new molecule in parallel. For example, a Gene(a,b) can produce a new protein in parallel by doing a transcribe reaction. (top) Stochastic behaviour is incorporated into the model by associating each reaction with a corresponding rate. The rate of a unary reaction is equal to the rate of the reaction name. The rate of a binary reaction is equal to the rate of the reaction channel. The rates are used as the basis for a stochastic simulation algorithm, which calculates the probability of all possible reactions at each step and stochastically chooses the next reaction based on these probabilities. What happens if we simulate one copy of the gene? *** [type this example into SPiM, hiding the existing text. Add sample and plot directives. Ask students to guess what will happen. Run the simulation] [Short version] (middle) The program describes the dynamic behaviour of the Gene. Each node in the graph represents a separate molecule in a given state. The gene can be on or off, and the protein can be active or degraded. Each labelled edge in the graph represents a reaction. The gene can produce proteins, which can degrade, or the gene can become blocked and then unblocked. [Background] Each node in the graph represents the state of a component, and each labelled edge represents a reaction, which can be either unary or binary. Unary reactions such as degradation are labelled with a reaction name. Binary reactions such as binding and unbinding are labelled with a reaction channel preceded by an input (?) or output (!) prefix. Two components can interact by doing a complementary input and output on the same channel. Each reaction name or channel is associated with a corresponding rate, which denotes the speed of the reaction. @1 , ?   v k  8 B+ [   3380___PPT10.[dqu   (    f9 y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZPP  d   ~ : y˼y˼?Rectangle 3]C  d A gene by itself produces a steady population of proteins. *** [click on Results icon. Show the sequence of reductions. Mention that the time is calculated based on the rate]    3380___PPT10.[dq  @(    f$ y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZPP  dt   ~% y˼y˼?Rectangle 3]C  d NSimulator does one reaction at a time. How does it decide which reaction happens next? The probability of a reaction is proportional to its rate. Add up the rates of all the reactions in the system, in order to calculate the probability. Duration of the reaction is calculated based on the total rate of the system. time 10*ln(1/n)O ? O  3380___PPT10.[dq  C;`#(    f' y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZPP  d   ~( y˼y˼?Rectangle 3]C  d R    3380___PPT10.[dq  C; #(      f* y˼y˼?Rectangle 7b   j*   a    r0e0e?Rectangle 2ZPP  d    ~+ y˼y˼?Rectangle 3]C  d R    3380___PPT10.[dq  C;#(    f- y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZPP  d   ~. y˼y˼?Rectangle 3]C  d R    3380___PPT10.[dq  C;#(    f y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZPP  d   ~ y˼y˼?Rectangle 3]C  d R    3380___PPT10.[dq  C;#(    f y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZPP  d   ~ y˼y˼?Rectangle 3]C  d R    3380___PPT10.[dq  c[C(    f` y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZPP  d8   ~` y˼y˼?Rectangle 3]C  d rWe used our model of a gene to program a biological clock, which was previously engineered in real bacteria. This is a famous experiment, that showed how we can  program real bacteria by inserting new genes into the bacteria. Done by Elowitz and Leibler. The clock uses a network of three genes similar to the one described previously. An extra gene was also inserted to observe the oscillations. The gene produced a protein that makes the bacteria glow (GFP). Able to build this network using a simple combination of our genes with negative control. Reproduced the observed oscillations in our simulations. We can reproduce the bacteria glowing on an off. But we also observe the oscillation of the other proteins in the simulation, which we cannot directly observe in live bacteria. *** (We see that GFP population is high when there is no Tet protein, since GFP is inhibited by Tet.) [Details:] This is a famous experiment, that showed how we can  program real bacteria by inserting new genes into the bacteria. Done by Elowitz and Leibler. Recall that a gene is a sequence of DNA that codes for a particular protein. Each gene has a promoter unit that allows the code to be read. If the promoter region is blocked, say by another protein, the gene can no longer be read and we say that it is  switched off . Experiment inserts specific genes into bacteria, which produce proteins that  switch each other off . Here we have three genes, tet, lambda and lac. tet produces a protein that blocks lambda, which in turn produces a protein that blocks lac, which in turn produces a protein that blocks tet. Form a cycle. An additional gene produces a green fluorescent protein (GFP). Makes the bacteria glow. Repressed by the Tet protein. This means that when the Tet protein is produced, it blocks the production of the GFP. Put these together, and what hapens? The bacteria glow on and off. Continue glowing in their descendents. Why? The network can be modelled and simulated in the stochastic pi-calculus, using a simple combination of three genes with negative control, as shown on the right. The simulations result in alternate oscillation of protein populations. We also see that GFP is high when there is no Tet protein, since GFP is inhibited by Tet. @ P `  B  :` C   3380___PPT10.SPĺ  g_  G(      f@ y˼y˼?Rectangle 7b   j*   a    r0e0e?Rectangle 2ZQQ  d<    ~2 y˼y˼?Rectangle 3]C  d v This gives rise to oscillations.! ! !  3380___PPT10.}5  H@@$((  $ $ f` y˼y˼?Rectangle 7b   j*   a $  r0e0e?Rectangle 2ZPP  d $  ~ y˼y˼?Rectangle 3]C  d WWe can debug our model to try to understand why the oscillations are produced in a particular order. 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[Details:] This video shows an example of a gene network, which consists of three genes that inhibit each other. The network is modelled in the stochastic pi-calculus, and displayed in 3D. The three genes in the model produce red, purple and blue proteins, respectively, where the genes are shown at the bottom level and the proteins are shown at the top. The genes can be in two states, either on or off, while the population of proteins can grow or shrink over time. When the gene is switched on, it produces proteins at a steady rate. The proteins can also degrade, so that the population of proteins stabilises when production and degradation are in equilibrium. The proteins can also interact with the genes, switching them on or off. The red gene produces proteins that switch off the purple gene, which produces proteins that switch off the blue gene, which produces proteins that switch off the red gene, completing the cycle. [run through the video, and pause at each point] The video shows how the gene network can produce oscillations in protein levels. Initially there is a large population of red proteins, which switch off the purple gene (1). The blue gene then starts producing proteins, which switch off the red gene (2). Since no more red proteins are produced, the population of red proteins slowly decreases over time, until all of the red proteins are degraded (3). The purple gene then starts producing proteins, which switch off the blue gene (4). Since no more blue proteins are produced, the population of blue proteins slowly decreases over time, until all of the blue proteins are degraded (5). The red gene then starts producing proteins, which switch off the purple gene, completing the cycle. We have several genetic oscillators inside our body, including one that controls our biological clock. These oscillators can be quite sophisticated, and computer models can help us understand how they work. *** Further detail: In the demo there are three separate promoter-gene units with negative control, one each for red, purple and blue proteins. The units are arranged in a cycle so that they mutually repress each other, as in the original Repressilator network. There are two types of nodes. Orange nodes represent reactions, and are of fixed size. Each reaction node is labelled with a reaction name, which can be either a delay at a given rate, an input on a channel or an output on a channel. The name of the reaction is displayed when clicking on the corresponding node. Nodes that are not orange represent species, and are of variable size, where the diameter of the node is proportional to the population of the species. The name of the species is displayed when clicking on the corresponding node. In this example there are two levels of species nodes. The nodes at the bottom level represent genes, which can be either on or off, while the nodes at the top level represent proteins, which can have variable populations. There are two types of edges. Yellow edges represent reactions, and go from a source species node to a reaction node, and from a reaction node to zero or more target species nodes. Green edges represent interactions between species, and go from an output reaction node on a given channel to a corresponding input reaction node on the same channel. Consider the red promoter gene unit in the example. The species Neg(lambda,lac) and Blocked(lambda,lac) are on the bottom right and left, respectively, while species Protein(lac) is on the top right. The gene can actively transcribe a protein by doing a delay, represented as a vertical edge to a reaction node "transcribe". This node has two outbound edges, one upward edge to Protein(lac) and another downward edge back to Neg(lambda,lac) (unfortunately the downward edge is not clearly visible). The gene can also be switched off by interacting with a blue protein on reaction node "?lambda" and going into a state Blocked(lambda,lac). The blocked gene can spontaneously unblock by doing a delay on reaction node "unblock". The transcribed protein can also degrade by doing a delay on reaction node "degrade", which has no outbound edges. The red protein can also block the purple gene by doing an output on reaction node "!lac" (this is mostly hidden from view, but can be observed by rotating the network in three dimensions). The purple gene is modelled by node Neg(lac,tet) while the blue jean is modelled by node Neg(tet,lambda). The interactions between genes and proteins give rise to alternate oscillations in protein populations.  PR[  )    3380___PPT10.+K  P(  P P f y˼y˼?Rectangle 7b   j*   a P  r0e0e?Rectangle 2ZPP  d P  ~ y˼y˼?Rectangle 3]C  d In some conditions the clock behaves irregularly. The gene can unblock, and cause a leaky transcription, which perturbs the signal.     3380___PPT10.=|(V  ?7T(  T T f y˼y˼?Rectangle 7b   j*   a T  r0e0e?Rectangle 2ZPP  d T  ~ y˼y˼?Rectangle 3]C  d NWe can improve the performance of the clock by changing our model of a gene. In this case, we require two proteins to form a dimer in order to block a gene. We can do this without changing the definition of the network. Allows modular programming.    3380___PPT10.c)  X(  X X f y˼y˼?Rectangle 7b   j*   a X  r0e0e?Rectangle 2ZPP  d~ X  ~ y˼y˼?Rectangle 3]C  d bWe obtain more regular oscillations with this form of cooperativity. Less sensitive to leaky transcription, since two proteins are required to block a gene. Even better whene we require tetramers instead of dimers. So the idea is that if we want to build a biological oscillator, computer simulations can help us to uncover the basic design principles. c c c  3380___PPT10.=ȩt;  \(  \ \ f  y˼y˼?Rectangle 7b   j*   a \  r0e0e?Rectangle 2ZQQ  d \  ~@ y˼y˼?Rectangle 3]C  d tSome of the researchers who designed the clock inside bacteria also engineered logic gates! [Details:] Same three genes: lac, lambda and tet, which produce Lac, Lambda and Tet proteins, respectively. Now, each gene has one of 5 possible promoters. Recall that each promoter allows the gene to be transcribed to a protein. Two of the promoters are blocked by Lac at different strengths, one promoter is blocked by Tet, one is blocked by lambda and one is enhanced by lambda. 3 different genes, 5 possible promoters, gives rise to 125 possible different networks of 3 promoter-gene units. Digital input: IPTG neutralises the Tet protein, and aTc neutralises the Lac protein. Digital output: GFP is linked to lambda. So if there is lambda, then there is no GFP and the bacteria glows. Put all of these circuits inside bacteria, and looked at those that behaved like boolean gates.u u u  3380___PPT10.5  0`|(  ` ` f y˼y˼?Rectangle 7b   j*   a `  r0e0e?Rectangle 2ZPP  dq `  ~ y˼y˼?Rectangle 3]C  d UIn order to model these logic gates, we defined a gene with an additional input that allows the protein to be inhibited. So we have two levels: the gene itself can be switched off, or the protein it produces can be inhibited. The presence of an inhibitor is used as an input to the system. [run simulation both with and without inhibitor] V V V  3380___PPT10.[dq  Pdu(  d d fѸ y˼y˼?Rectangle 7b   j*   a d  r0e0e?Rectangle 2ZQQ  dj d  ~`и y˼y˼?Rectangle 3]C  d NWe can model 125 networks with just 2 modules. Illustrates one of the benefits of our approach. Can change the definition of a gate, without changing top-level network. Computer simulations can help us program logic gates in bacteria. Once you have logic gates, you are one step closer to having a biological computer. In the long-term, if we ever want to design biological hardware we will need a way of specifying and verifying our designs. Requires specialised tools for modelling concurrent, stochastic systems. [Details:] [show simulations with the 4 types of input] Boolean input simulated by presence or absence of inhibitors. Boolean output simulated by presence or absence of GFP Intuitive boolean analysis does not reproduce the experiment. [explain why, by reverse analysis, we get a contradiction in absence of inhibitors] We need to understand the dynamics of the head feedback loop. [show simulation of cascade without head feedback] Ask audience to guess [show simulation of head feedback, and how we can obtain a fixpoint] [show simulation with different values of unblocking, in absence of inhibitors] [see paper:  A compositional approach to the stochastic dynamics of gene networks ] Shows how the pi-calculus is a useful framework for modelling combinatorics: we can reproduce the combinatorial aspect of the in-vivo experiments. Also shows how insight can be gained simply by playing around with circuits and observing the results. Can formulate hypotheses about behaviour of networks by using different combinations of genes. The main point was to show how we can build complex networks from simple building blocks. Modular construction made it easier to experiment with different circuits. Simple boolean analysis does not predict the experiments. Need to take into account the dynamics of the circuit, in the presence of noise, in order to explain some of the results. *Here we showed that the unexpected experimental results can be reproduced when the head feedback loop of the tet gene is at a fixpoint. We can reproduce the experimental results. In the case of D038, we can perform experiments in silico to explain the regime of operation of the circuit. In particular, the experimental results are only reproduced in certain regimes. Do not have the rates. But can perform experiments to formulate hypotheses about what conditions are required in order to reproduce the experiments. N.B. Once we have defined the libraries, we can forget about them and just code up the network using calls to the library. Two kinds of programmers: library developers, and library users. Proteins aTc and IPTG act as boolean inputs. GFP as boolean output. Either the bacteria glows or it doesn t.      3380___PPT10.0  ph(  h h f y˼y˼?Rectangle 7b   j*   a h  r0e0e?Rectangle 2ZPP  d h  ~ y˼y˼?Rectangle 3]C  d For one of our main projects we have teamed up with leading researchers in Immunology, to model a key pathway of our immune system.     33  l(  l l fӸ y˼y˼?Rectangle 7b   j*   a l  r0e0e?Rectangle 2ZPP  dw l  ~Ը y˼y˼?Rectangle 3]C  d WThe detection is performed by a special protein complex called MHC, which acts like a biological anti-virus mechanism. The complex sits inside a special compartment of the cell, and regularly scans a sample of the protein fragments that are present inside the cell. The complex is able to recognise and capture the fragments that are potentially harmful, e.g. from a virus or bacterium living inside the cell. The captured fragments are presented at the cell surface, as evidence that the cell is infected. The fragments at the surface are recognised as harmful, and the infected cell is destroyed. X XX   33  A9p!(  p p f@ y˼y˼?Rectangle 7b   j*   a p  r0e0e?Rectangle 2ZPP  d p  ~ָ y˼y˼?Rectangle 3]C  d PThe main goal of our project was to understand the role of one of the key molecules in the system, called Tapasin. We are currently collaborating with leading researchers in Immunology and Structural Biology from Southampton University (UK), in order to understand how the system functions. In particular, we are trying to understand the role of one of the key molecules in the system, called Tapasin. [Details] Leading researchers in Immunology and Structural Biology from Southampton University (UK) have been studying MHC I antigen presentation for many years, in order to understand how the MHC complex is able to capture the right peptides. In particular, they have been trying to understand the role of Tapasin on peptide editing. [next] We are currently collaborating with these researchers, in order to develop a computer model that captures their current knowledge of MHC I antigen presentation. We are also including additional hypotheses, and running computer simulations of the model.     33  7/t(  t t f߸ y˼y˼?Rectangle 7b   j*   a t  r0e0e?Rectangle 2ZPP  d  t  ~ݸ y˼y˼?Rectangle 3]C  d FdWe teamed up with these scientists to develop a computer model that captures their knowledge about the system. We also included some additional hypotheses, and ran computer simulations of the model. [Explain the model] This slide presents a stochastic pi-calculus model of peptide loading by MHC I. Each connected graph in the figure describes the behaviour of a component in the system. There are graphs for peptide (a), tapasin (b) and MHC (c). Each node in the graph represents a component state and each directed edge represents a reaction, which can be either unary or binary. Unary reactions such as degradation are labelled with the reaction rate. Binary reactions such as association and dissociation are labelled with an interaction channel preceeded by an input (?) or output (!) prefix, where each channel is associated with a corresponding interaction rate. Two components can interact by doing a complementary input and output on the same channel, where the rate of the interaction is equal to the rate of the channel. a) Peptides are actively loaded into the ER at rate generate_pep, and are degraded at rate degrade_pep. Each peptide is characterised by a private channel u, whose rate determines its affinity to MHC. We assume an equal supply of three classes of peptides with low, medium and high unbinding rates, resulting in high, medium and low affinity peptides, respectively. A peptide can bind to an MHC complex by doing an output on channel bind. The bound peptide can then unbind from MHC by doing an input on channel u. b) Tapasin is assembled in the ER at rate generate_TPN, and is degraded at rate degrade_TPN. Each tapasin molecule is characterised by a private channel uT, whose rate determines its affinity to MHC. Tapasin can bind to MHC by doing an output on channel bindT. The bound tapasin can then unbind from MHC by doing an input on channel uT. c) MHC is assembled in the ER at rate generate_MHC, and is degraded at rate degrade_MHCo. Free MHC can load a peptide with affinity u by doing an input on channel bind. The loaded MHC can then release the peptide by doing an output on channel u. The rate of unbinding is determined by the rate of the channel, which can be low, medium or high, depending on the nature of the loaded peptide. Loaded MHC can egress to the cell surface at rate egress, where it is degraded at rate degrade_MHCe. Free MHC in the ER can also bind to tapasin by doing an input on channel bindT. The bound MHC can then unbind by doing an output on channel uT. The rate of unbinding of empty MHC from tapasin is determined by the rate of channel uT, multiplied by a constant factor v. MHC can also load a peptide in presence of tapasin. We assume that loaded MHC can only egress in absence of tapasin, since tapasin has an ER retention signal. We neglect the degradation of empty MHC bound to tapasin, which is in the order of two hours, and of loaded MHC, which is in the order of several hours []. [explain model of effect of tapasin on loading] We want to study the effect of tapasin on peptide loading. Allow tapasin to affect all aspects of loading. The effects are modelled by multiplying the rates of binding and unbinding of peptide to MHC by a constant factor. As a result a number of different functions of Tapasin can be modelled in isolation or in combination. For example an increase in the binding rate of peptides to MHC would model the stabilisation of the open MHC complex. Tapasin can also decrease the unbinding rate of peptides from MHC by improving the stability of closed MHC complexes. Finally, a peptide can increase the affinity of Tapasin to MHC, by inducing a conformational change in MHC.^  P  P - " 4      5    J  -      >  c  J  *      ,    L       K  >  W  "  = " L -  Y    3380___PPT10. JD  7/x(  x x f@ y˼y˼?Rectangle 7b   j*   a x  r0e0e?Rectangle 2ZPP  d  x  ~ y˼y˼?Rectangle 3]C  d FdWe teamed up with these scientists to develop a computer model that captures their knowledge about the system. We also included some additional hypotheses, and ran computer simulations of the model. [Explain the model] This slide presents a stochastic pi-calculus model of peptide loading by MHC I. Each connected graph in the figure describes the behaviour of a component in the system. There are graphs for peptide (a), tapasin (b) and MHC (c). Each node in the graph represents a component state and each directed edge represents a reaction, which can be either unary or binary. Unary reactions such as degradation are labelled with the reaction rate. Binary reactions such as association and dissociation are labelled with an interaction channel preceeded by an input (?) or output (!) prefix, where each channel is associated with a corresponding interaction rate. Two components can interact by doing a complementary input and output on the same channel, where the rate of the interaction is equal to the rate of the channel. a) Peptides are actively loaded into the ER at rate generate_pep, and are degraded at rate degrade_pep. Each peptide is characterised by a private channel u, whose rate determines its affinity to MHC. We assume an equal supply of three classes of peptides with low, medium and high unbinding rates, resulting in high, medium and low affinity peptides, respectively. A peptide can bind to an MHC complex by doing an output on channel bind. The bound peptide can then unbind from MHC by doing an input on channel u. b) Tapasin is assembled in the ER at rate generate_TPN, and is degraded at rate degrade_TPN. Each tapasin molecule is characterised by a private channel uT, whose rate determines its affinity to MHC. Tapasin can bind to MHC by doing an output on channel bindT. The bound tapasin can then unbind from MHC by doing an input on channel uT. c) MHC is assembled in the ER at rate generate_MHC, and is degraded at rate degrade_MHCo. Free MHC can load a peptide with affinity u by doing an input on channel bind. The loaded MHC can then release the peptide by doing an output on channel u. The rate of unbinding is determined by the rate of the channel, which can be low, medium or high, depending on the nature of the loaded peptide. Loaded MHC can egress to the cell surface at rate egress, where it is degraded at rate degrade_MHCe. Free MHC in the ER can also bind to tapasin by doing an input on channel bindT. The bound MHC can then unbind by doing an output on channel uT. The rate of unbinding of empty MHC from tapasin is determined by the rate of channel uT, multiplied by a constant factor v. MHC can also load a peptide in presence of tapasin. We assume that loaded MHC can only egress in absence of tapasin, since tapasin has an ER retention signal. We neglect the degradation of empty MHC bound to tapasin, which is in the order of two hours, and of loaded MHC, which is in the order of several hours []. [explain model of effect of tapasin on loading] We want to study the effect of tapasin on peptide loading. Allow tapasin to affect all aspects of loading. The effects are modelled by multiplying the rates of binding and unbinding of peptide to MHC by a constant factor. As a result a number of different functions of Tapasin can be modelled in isolation or in combination. For example an increase in the binding rate of peptides to MHC would model the stabilisation of the open MHC complex. Tapasin can also decrease the unbinding rate of peptides from MHC by improving the stability of closed MHC complexes. Finally, a peptide can increase the affinity of Tapasin to MHC, by inducing a conformational change in MHC.^  P  P - " 4      5    J  -      >  c  J  *      ,    L       K  >  W  "  = " L -  Y    3380___PPT10. JD  7/ |(  | | f3 y˼y˼?Rectangle 7b   j*   a |  r0e0e?Rectangle 2ZPP  d  |  ~ y˼y˼?Rectangle 3]C  d FdWe teamed up with these scientists to develop a computer model that captures their knowledge about the system. We also included some additional hypotheses, and ran computer simulations of the model. [Explain the model] This slide presents a stochastic pi-calculus model of peptide loading by MHC I. Each connected graph in the figure describes the behaviour of a component in the system. There are graphs for peptide (a), tapasin (b) and MHC (c). Each node in the graph represents a component state and each directed edge represents a reaction, which can be either unary or binary. Unary reactions such as degradation are labelled with the reaction rate. Binary reactions such as association and dissociation are labelled with an interaction channel preceeded by an input (?) or output (!) prefix, where each channel is associated with a corresponding interaction rate. Two components can interact by doing a complementary input and output on the same channel, where the rate of the interaction is equal to the rate of the channel. a) Peptides are actively loaded into the ER at rate generate_pep, and are degraded at rate degrade_pep. Each peptide is characterised by a private channel u, whose rate determines its affinity to MHC. We assume an equal supply of three classes of peptides with low, medium and high unbinding rates, resulting in high, medium and low affinity peptides, respectively. A peptide can bind to an MHC complex by doing an output on channel bind. The bound peptide can then unbind from MHC by doing an input on channel u. b) Tapasin is assembled in the ER at rate generate_TPN, and is degraded at rate degrade_TPN. Each tapasin molecule is characterised by a private channel uT, whose rate determines its affinity to MHC. Tapasin can bind to MHC by doing an output on channel bindT. The bound tapasin can then unbind from MHC by doing an input on channel uT. c) MHC is assembled in the ER at rate generate_MHC, and is degraded at rate degrade_MHCo. Free MHC can load a peptide with affinity u by doing an input on channel bind. The loaded MHC can then release the peptide by doing an output on channel u. The rate of unbinding is determined by the rate of the channel, which can be low, medium or high, depending on the nature of the loaded peptide. Loaded MHC can egress to the cell surface at rate egress, where it is degraded at rate degrade_MHCe. Free MHC in the ER can also bind to tapasin by doing an input on channel bindT. The bound MHC can then unbind by doing an output on channel uT. The rate of unbinding of empty MHC from tapasin is determined by the rate of channel uT, multiplied by a constant factor v. MHC can also load a peptide in presence of tapasin. We assume that loaded MHC can only egress in absence of tapasin, since tapasin has an ER retention signal. We neglect the degradation of empty MHC bound to tapasin, which is in the order of two hours, and of loaded MHC, which is in the order of several hours []. [explain model of effect of tapasin on loading] We want to study the effect of tapasin on peptide loading. Allow tapasin to affect all aspects of loading. The effects are modelled by multiplying the rates of binding and unbinding of peptide to MHC by a constant factor. As a result a number of different functions of Tapasin can be modelled in isolation or in combination. For example an increase in the binding rate of peptides to MHC would model the stabilisation of the open MHC complex. Tapasin can also decrease the unbinding rate of peptides from MHC by improving the stability of closed MHC complexes. Finally, a peptide can increase the affinity of Tapasin to MHC, by inducing a conformational change in MHC.^  P  P - " 4      5    J  -      >  c  J  *      ,    L       K  >  W  "  = " L -  Y    3380___PPT10. JD  7/0 (    f y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZPP  d    ~ y˼y˼?Rectangle 3]C  d FdWe teamed up with these scientists to develop a computer model that captures their knowledge about the system. We also included some additional hypotheses, and ran computer simulations of the model. [Explain the model] This slide presents a stochastic pi-calculus model of peptide loading by MHC I. Each connected graph in the figure describes the behaviour of a component in the system. There are graphs for peptide (a), tapasin (b) and MHC (c). Each node in the graph represents a component state and each directed edge represents a reaction, which can be either unary or binary. Unary reactions such as degradation are labelled with the reaction rate. Binary reactions such as association and dissociation are labelled with an interaction channel preceeded by an input (?) or output (!) prefix, where each channel is associated with a corresponding interaction rate. Two components can interact by doing a complementary input and output on the same channel, where the rate of the interaction is equal to the rate of the channel. a) Peptides are actively loaded into the ER at rate generate_pep, and are degraded at rate degrade_pep. Each peptide is characterised by a private channel u, whose rate determines its affinity to MHC. We assume an equal supply of three classes of peptides with low, medium and high unbinding rates, resulting in high, medium and low affinity peptides, respectively. A peptide can bind to an MHC complex by doing an output on channel bind. The bound peptide can then unbind from MHC by doing an input on channel u. b) Tapasin is assembled in the ER at rate generate_TPN, and is degraded at rate degrade_TPN. Each tapasin molecule is characterised by a private channel uT, whose rate determines its affinity to MHC. Tapasin can bind to MHC by doing an output on channel bindT. The bound tapasin can then unbind from MHC by doing an input on channel uT. c) MHC is assembled in the ER at rate generate_MHC, and is degraded at rate degrade_MHCo. Free MHC can load a peptide with affinity u by doing an input on channel bind. The loaded MHC can then release the peptide by doing an output on channel u. The rate of unbinding is determined by the rate of the channel, which can be low, medium or high, depending on the nature of the loaded peptide. Loaded MHC can egress to the cell surface at rate egress, where it is degraded at rate degrade_MHCe. Free MHC in the ER can also bind to tapasin by doing an input on channel bindT. The bound MHC can then unbind by doing an output on channel uT. The rate of unbinding of empty MHC from tapasin is determined by the rate of channel uT, multiplied by a constant factor v. MHC can also load a peptide in presence of tapasin. We assume that loaded MHC can only egress in absence of tapasin, since tapasin has an ER retention signal. We neglect the degradation of empty MHC bound to tapasin, which is in the order of two hours, and of loaded MHC, which is in the order of several hours []. [explain model of effect of tapasin on loading] We want to study the effect of tapasin on peptide loading. Allow tapasin to affect all aspects of loading. The effects are modelled by multiplying the rates of binding and unbinding of peptide to MHC by a constant factor. As a result a number of different functions of Tapasin can be modelled in isolation or in combination. For example an increase in the binding rate of peptides to MHC would model the stabilisation of the open MHC complex. Tapasin can also decrease the unbinding rate of peptides from MHC by improving the stability of closed MHC complexes. Finally, a peptide can increase the affinity of Tapasin to MHC, by inducing a conformational change in MHC.^  P  P - " 4      5    J  -      >  c  J  *      ,    L       K  >  W  "  = " L -  Y    3380___PPT10. JD  7/P (    f y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZPP  d    ~ y˼y˼?Rectangle 3]C  d FdWe teamed up with these scientists to develop a computer model that captures their knowledge about the system. We also included some additional hypotheses, and ran computer simulations of the model. [Explain the model] This slide presents a stochastic pi-calculus model of peptide loading by MHC I. Each connected graph in the figure describes the behaviour of a component in the system. There are graphs for peptide (a), tapasin (b) and MHC (c). Each node in the graph represents a component state and each directed edge represents a reaction, which can be either unary or binary. Unary reactions such as degradation are labelled with the reaction rate. Binary reactions such as association and dissociation are labelled with an interaction channel preceeded by an input (?) or output (!) prefix, where each channel is associated with a corresponding interaction rate. Two components can interact by doing a complementary input and output on the same channel, where the rate of the interaction is equal to the rate of the channel. a) Peptides are actively loaded into the ER at rate generate_pep, and are degraded at rate degrade_pep. Each peptide is characterised by a private channel u, whose rate determines its affinity to MHC. We assume an equal supply of three classes of peptides with low, medium and high unbinding rates, resulting in high, medium and low affinity peptides, respectively. A peptide can bind to an MHC complex by doing an output on channel bind. The bound peptide can then unbind from MHC by doing an input on channel u. b) Tapasin is assembled in the ER at rate generate_TPN, and is degraded at rate degrade_TPN. Each tapasin molecule is characterised by a private channel uT, whose rate determines its affinity to MHC. Tapasin can bind to MHC by doing an output on channel bindT. The bound tapasin can then unbind from MHC by doing an input on channel uT. c) MHC is assembled in the ER at rate generate_MHC, and is degraded at rate degrade_MHCo. Free MHC can load a peptide with affinity u by doing an input on channel bind. The loaded MHC can then release the peptide by doing an output on channel u. The rate of unbinding is determined by the rate of the channel, which can be low, medium or high, depending on the nature of the loaded peptide. Loaded MHC can egress to the cell surface at rate egress, where it is degraded at rate degrade_MHCe. Free MHC in the ER can also bind to tapasin by doing an input on channel bindT. The bound MHC can then unbind by doing an output on channel uT. The rate of unbinding of empty MHC from tapasin is determined by the rate of channel uT, multiplied by a constant factor v. MHC can also load a peptide in presence of tapasin. We assume that loaded MHC can only egress in absence of tapasin, since tapasin has an ER retention signal. We neglect the degradation of empty MHC bound to tapasin, which is in the order of two hours, and of loaded MHC, which is in the order of several hours []. [explain model of effect of tapasin on loading] We want to study the effect of tapasin on peptide loading. Allow tapasin to affect all aspects of loading. The effects are modelled by multiplying the rates of binding and unbinding of peptide to MHC by a constant factor. As a result a number of different functions of Tapasin can be modelled in isolation or in combination. For example an increase in the binding rate of peptides to MHC would model the stabilisation of the open MHC complex. Tapasin can also decrease the unbinding rate of peptides from MHC by improving the stability of closed MHC complexes. Finally, a peptide can increase the affinity of Tapasin to MHC, by inducing a conformational change in MHC.^  P  P - " 4      5    J  -      >  c  J  *      ,    L       K  >  W  "  = " L -  Y    3380___PPT10. JD  7/p (    f`p y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZPP  d    ~ y˼y˼?Rectangle 3]C  d FdWe teamed up with these scientists to develop a computer model that captures their knowledge about the system. We also included some additional hypotheses, and ran computer simulations of the model. [Explain the model] This slide presents a stochastic pi-calculus model of peptide loading by MHC I. Each connected graph in the figure describes the behaviour of a component in the system. There are graphs for peptide (a), tapasin (b) and MHC (c). Each node in the graph represents a component state and each directed edge represents a reaction, which can be either unary or binary. Unary reactions such as degradation are labelled with the reaction rate. Binary reactions such as association and dissociation are labelled with an interaction channel preceeded by an input (?) or output (!) prefix, where each channel is associated with a corresponding interaction rate. Two components can interact by doing a complementary input and output on the same channel, where the rate of the interaction is equal to the rate of the channel. a) Peptides are actively loaded into the ER at rate generate_pep, and are degraded at rate degrade_pep. Each peptide is characterised by a private channel u, whose rate determines its affinity to MHC. We assume an equal supply of three classes of peptides with low, medium and high unbinding rates, resulting in high, medium and low affinity peptides, respectively. A peptide can bind to an MHC complex by doing an output on channel bind. The bound peptide can then unbind from MHC by doing an input on channel u. b) Tapasin is assembled in the ER at rate generate_TPN, and is degraded at rate degrade_TPN. Each tapasin molecule is characterised by a private channel uT, whose rate determines its affinity to MHC. Tapasin can bind to MHC by doing an output on channel bindT. The bound tapasin can then unbind from MHC by doing an input on channel uT. c) MHC is assembled in the ER at rate generate_MHC, and is degraded at rate degrade_MHCo. Free MHC can load a peptide with affinity u by doing an input on channel bind. The loaded MHC can then release the peptide by doing an output on channel u. The rate of unbinding is determined by the rate of the channel, which can be low, medium or high, depending on the nature of the loaded peptide. Loaded MHC can egress to the cell surface at rate egress, where it is degraded at rate degrade_MHCe. Free MHC in the ER can also bind to tapasin by doing an input on channel bindT. The bound MHC can then unbind by doing an output on channel uT. The rate of unbinding of empty MHC from tapasin is determined by the rate of channel uT, multiplied by a constant factor v. MHC can also load a peptide in presence of tapasin. We assume that loaded MHC can only egress in absence of tapasin, since tapasin has an ER retention signal. We neglect the degradation of empty MHC bound to tapasin, which is in the order of two hours, and of loaded MHC, which is in the order of several hours []. [explain model of effect of tapasin on loading] We want to study the effect of tapasin on peptide loading. Allow tapasin to affect all aspects of loading. The effects are modelled by multiplying the rates of binding and unbinding of peptide to MHC by a constant factor. As a result a number of different functions of Tapasin can be modelled in isolation or in combination. For example an increase in the binding rate of peptides to MHC would model the stabilisation of the open MHC complex. Tapasin can also decrease the unbinding rate of peptides from MHC by improving the stability of closed MHC complexes. Finally, a peptide can increase the affinity of Tapasin to MHC, by inducing a conformational change in MHC.^  P  P - " 4      5    J  -      >  c  J  *      ,    L       K  >  W  "  = " L -  Y    3380___PPT10. JD  7/ (    f`s y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZPP  d    ~q y˼y˼?Rectangle 3]C  d FdWe teamed up with these scientists to develop a computer model that captures their knowledge about the system. We also included some additional hypotheses, and ran computer simulations of the model. [Explain the model] This slide presents a stochastic pi-calculus model of peptide loading by MHC I. Each connected graph in the figure describes the behaviour of a component in the system. There are graphs for peptide (a), tapasin (b) and MHC (c). Each node in the graph represents a component state and each directed edge represents a reaction, which can be either unary or binary. Unary reactions such as degradation are labelled with the reaction rate. Binary reactions such as association and dissociation are labelled with an interaction channel preceeded by an input (?) or output (!) prefix, where each channel is associated with a corresponding interaction rate. Two components can interact by doing a complementary input and output on the same channel, where the rate of the interaction is equal to the rate of the channel. a) Peptides are actively loaded into the ER at rate generate_pep, and are degraded at rate degrade_pep. Each peptide is characterised by a private channel u, whose rate determines its affinity to MHC. We assume an equal supply of three classes of peptides with low, medium and high unbinding rates, resulting in high, medium and low affinity peptides, respectively. A peptide can bind to an MHC complex by doing an output on channel bind. The bound peptide can then unbind from MHC by doing an input on channel u. b) Tapasin is assembled in the ER at rate generate_TPN, and is degraded at rate degrade_TPN. Each tapasin molecule is characterised by a private channel uT, whose rate determines its affinity to MHC. Tapasin can bind to MHC by doing an output on channel bindT. The bound tapasin can then unbind from MHC by doing an input on channel uT. c) MHC is assembled in the ER at rate generate_MHC, and is degraded at rate degrade_MHCo. Free MHC can load a peptide with affinity u by doing an input on channel bind. The loaded MHC can then release the peptide by doing an output on channel u. The rate of unbinding is determined by the rate of the channel, which can be low, medium or high, depending on the nature of the loaded peptide. Loaded MHC can egress to the cell surface at rate egress, where it is degraded at rate degrade_MHCe. Free MHC in the ER can also bind to tapasin by doing an input on channel bindT. The bound MHC can then unbind by doing an output on channel uT. The rate of unbinding of empty MHC from tapasin is determined by the rate of channel uT, multiplied by a constant factor v. MHC can also load a peptide in presence of tapasin. We assume that loaded MHC can only egress in absence of tapasin, since tapasin has an ER retention signal. We neglect the degradation of empty MHC bound to tapasin, which is in the order of two hours, and of loaded MHC, which is in the order of several hours []. [explain model of effect of tapasin on loading] We want to study the effect of tapasin on peptide loading. Allow tapasin to affect all aspects of loading. The effects are modelled by multiplying the rates of binding and unbinding of peptide to MHC by a constant factor. As a result a number of different functions of Tapasin can be modelled in isolation or in combination. For example an increase in the binding rate of peptides to MHC would model the stabilisation of the open MHC complex. Tapasin can also decrease the unbinding rate of peptides from MHC by improving the stability of closed MHC complexes. Finally, a peptide can increase the affinity of Tapasin to MHC, by inducing a conformational change in MHC.^  P  P - " 4      5    J  -      >  c  J  *      ,    L       K  >  W  "  = " L -  Y    3380___PPT10. JD   (    f y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZPP  dt   ~ y˼y˼?Rectangle 3]C  d >We assume an equal supply of three classes of peptides with low, medium and high unbinding rates, resulting in high, medium and low affinity MHC peptide complexes. Note that we do not change the model for MHC. It is parameterised by the class of peptide. Use the high affinity peptide as the representative peptide.  ? > >   3380___PPT10. JD  A9 !(    f t y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZPP  d   ~@u y˼y˼?Rectangle 3]C  d PRates. The whole process needs to take about 3 hours. The exact values of the rates is not critical. But the proportions are. For example, assume high peptide turnover. Assume 3 classes of peptides. How long does an MHC complex take to assemble, etc.    3380___PPT10.Vf  UM 5(     0e0e?4Slide Image Placeholder 1ZPP  d   v y˼y˼?(Notes Placeholder 2]C  d The simulations plot the number of harmful, moderetely harmful and harmless fragments that are presented at the cell surface. We see that there is a much higher proportion of harmful fragments are presented. [run simulation] Would you like to delete this last line? You ve just performed your first gene knockout experiment. We see that without tapasin, MHC presents a higher proportion of harmless peptides at the cell surface. So we can reproduce known experiments, but can we explain why?  /  w y˼y˼?6Slide Number Placeholder 3b   j*   a 33+   (    fy y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZPP  d   ~z y˼y˼?Rectangle 3]C  d We can used our debugging tools to try to understand how the system works. Here we try to explain why a higher proportion of harmful fragments are presented. The simulations were able to reproduce the observed experiments. The MHC presented a large proportion of stable peptides (red), some moderately stable peptide (blue) and very few unstable peptides (yellow) at the cell surface. How does our model achieve this?    334  @ (    f y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZPP  d   ~1 y˼y˼?Rectangle 3]C  d How does MHC capture the right peptide? Peptides that are recognised as harmful bind in a stable way to MHC. So ideally, MHC should wait an infinite amount of time before egressing to the cell surface, to be sure to capture the most stable peptides. Cannot wait indefinitely, since a decision needs to be taken quickly. But if MHC acts too quickly, it will take the first peptide that comes along. Need a trade-off between how effective we are and how quickly we can respond. Can calculate the upper bound as egression tends to infinity. [Details:] An open MHC complex can bind a free peptide by doing an input ?bind(u), where the affinity of the peptide is determined by channel u. The loaded MHC complex can either egress, or release the peptide by doing an output !u. n d  =  %  ,      3380___PPT10.~  y` a(    f} y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZPP  dV   ~~ y˼y˼?Rectangle 3]C  d 4Assume three classes of peptides: stable (high), moderately stable (med) and unstable (low). Can calculate upper and lower bounds of peptide descrimination as a function of waiting time, based on relative probabilities. [Details:] It is instructive to analyse the relative proportions of MHC peptide complexes with peptides of low, medium and high unbinding rates as a function of the rate of egression. In the simplest case we consider only MHC and peptide and will add tapsin later. As the rate of egression tends to zero the proportion of high, medium and low affinity MHC peptide complexes tends to the limiting ratios of 12/19, 5/19 and 2/19, respectively. This is expected as can be shown by analysing the probabilities of the formation of MHC peptide complexes as a function of the binding, unbinding and egression rates. If we assume that MHC complexes are loaded with an equal proportion of peptides with low, medium and high unbinding rates due to high peptide turnover, the probability of egression for a peptide with affinity u is given by the above equation.5 5 5   3380___PPT10.~^   (    f౽ y˼y˼?Rectangle 7b   j*   a   r0e0e?Rectangle 2ZPP  d   ~ y˼y˼?Rectangle 3]C  d Graph shows relative proportion of unstable (low), moderately stable (medium) and stable (high) peptides presented at the cell surface, as egression rate tends to zero (i.e. as waiting time tends to infinity) MHC cannnot tell the difference between peptides if it egresses immediately. Discrimination improves the longer it waits before egressing. Able to capture high affinity peptides more effectively.     3380___PPT10.   ~˽ y˼y˼?Rectangle 3]C  d x"v = 0.0. 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