Team:UESTC Life/Modeling
From 2013.igem.org
(→First Model) |
(→Second Model) |
||
Line 122: | Line 122: | ||
== '''Second Model ''' == | == '''Second Model ''' == | ||
- | The second model grade Linker and predict optimal length of linker in chimeric protein. According to many papers, the effects of linker length on equilibrium stability arise from significant and sometimes opposing changes in folding and unfolding kinetics.1,4,7,8 As for the structure, the rank of linker | + | The second model grade Linker and predict optimal length of linker in chimeric protein. According to many papers, the effects of linker length on equilibrium stability arise from significant and sometimes opposing changes in folding and unfolding kinetics.[1,4,7,8] As for the structure, the rank of linker is α-helix >β-sheet > loop.[2,3,4,5,8] And the effect of structure is dominant. We collected amass of data1,[4,6,7,8] and degraded the effect of linker. Finally, we got a formula. The formula can predict the efficiency of the length of linker. The full points is 10. |
=== '''Length points ''' === | === '''Length points ''' === | ||
<center>https://static.igem.org/mediawiki/2013/e/e4/Uestclifemod.jpg</center> | <center>https://static.igem.org/mediawiki/2013/e/e4/Uestclifemod.jpg</center> |
Revision as of 03:34, 27 September 2013
Modeling |
---|
Contents |
First Model
Our first model explored the change of intermediate product in multistep degradation of TCP. assume K1=1,K2=0.5,the reaction is TCP→2,3DCP+Cl- ; 2,3DCP→A+Cl-. Through matlab analyzing, the program was in the program bar. Finally, the reaction curve was predicted. The result was similar to what we had got through experiment.
FIG. The blue line stand for TCP; Red line stand for 2,3-DCP; Green line stand for serial product after 2,3-DCP.
Program
Second Model
The second model grade Linker and predict optimal length of linker in chimeric protein. According to many papers, the effects of linker length on equilibrium stability arise from significant and sometimes opposing changes in folding and unfolding kinetics.[1,4,7,8] As for the structure, the rank of linker is α-helix >β-sheet > loop.[2,3,4,5,8] And the effect of structure is dominant. We collected amass of data1,[4,6,7,8] and degraded the effect of linker. Finally, we got a formula. The formula can predict the efficiency of the length of linker. The full points is 10.
Length points
y=y0 + (A/(w*sqrt(PI/2)))*exp(-2*((x-xc)/w)^2)
Y0=4.19829; Xc=21.97825; W=13.10889; A=68.84675
Structure point
1.α-helix A 2.β-sheet B 3. loop C
Result s
The point of P2A is A, the length point is 7.9777 P2A is in high score in this system.
Predict
The optimal linker is an α-helix and the number of amino acid is 22. So in future work we can construct this linker.
Reference