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Chen, H; Zhou, X; Ou-Yang, ZC; Chen, H , Tsing Hua Univ, Ctr Adv Study, Beijing 100084, Peoples R China.
Secondary-structure-favored hydrophobic-polar lattice model of protein folding
Source PublicationPHYSICAL REVIEW E
KeywordPacking Density Cooperativity Superfamilies Designability Polymers Origins Chains
AbstractProtein folding studied using a two-dimensional lattice model with the Hamiltonian including both hydrophobic interactions and main chain hydrogen bond interactions of amino acids. Since compact conformations have different designabilities and only highly designable conformations can act as native structural candidates [H. Li, R. Helling, C. Tang, and N. Wingreen, Science 273, 666 (1996)], it is shown that hydrophobic interaction alone is insufficient to explain the appearance of a high proportion of regular secondary structures, especially beta sheets whose content decreases with increasing designability, but interactions of main chain hydrogen bonds can account for this. Thus the emergence of only a small number of structure types (folds) among all possible structures can be understood to some extent.
2001
ISSN1063-651X
Volume64Issue:4Pages:-
Subject AreaPhysics
Indexed BySCI
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Document Type期刊论文
Identifierhttp://ir.itp.ac.cn/handle/311006/13659
Collection理论物理所科研产出_SCI论文
Corresponding AuthorChen, H , Tsing Hua Univ, Ctr Adv Study, Beijing 100084, Peoples R China.
Recommended Citation
GB/T 7714
Chen, H,Zhou, X,Ou-Yang, ZC,et al. Secondary-structure-favored hydrophobic-polar lattice model of protein folding[J]. PHYSICAL REVIEW E,2001,64(4):-.
APA Chen, H,Zhou, X,Ou-Yang, ZC,&Chen, H , Tsing Hua Univ, Ctr Adv Study, Beijing 100084, Peoples R China..(2001).Secondary-structure-favored hydrophobic-polar lattice model of protein folding.PHYSICAL REVIEW E,64(4),-.
MLA Chen, H,et al."Secondary-structure-favored hydrophobic-polar lattice model of protein folding".PHYSICAL REVIEW E 64.4(2001):-.
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