Medium effects on the selection of sequences folding into stable proteins in a simple model.
We study the medium effects on the selection of sequences in protein folding by taking into account surface potential in hydrophobic-polar model. Our numerical calculation demonstrates that the surface potential enhances the average gap for the highly designable structures. It also shows that the most stable structure may be no longer the most stable one if the medium is changed.
Li
You-Quan
YQ
Department of Physics, Zhejiang University, Hangzhou 310027, People's Republic of China.
Ji
Yong-Yun
YY
Mao
Jun-Wen
JW
Tang
Xiao-Wei
XW
D000595:Amino Acid Sequence; D003198:Computer Simulation; D003470:Culture Media / Q000737:chemistry*; D008956:Models, Chemical; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D020539:Sequence Analysis, Protein / Q000379:methods*; D012996:Solutions; D012997:Solvents / Q000737:chemistry*; D013329:Structure-Activity Relationship
D003470:Culture Media; D012996:Solutions; D012997:Solvents