中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Secondary-structure-favored hydrophobic-polar lattice model of protein folding

文献类型:期刊论文

作者Chen, H; Zhou, X; Ou-Yang, ZC; Chen, H , Tsing Hua Univ, Ctr Adv Study, Beijing 100084, Peoples R China.
刊名PHYSICAL REVIEW E
出版日期2001
卷号64期号:4页码:-
关键词Packing Density Cooperativity Superfamilies Designability Polymers Origins Chains
ISSN号1063-651X
英文摘要Protein 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.
学科主题Physics
WOS记录号WOS:000171649000052
公开日期2012-08-29
源URL[http://ir.itp.ac.cn/handle/311006/13659]  
专题理论物理研究所_理论物理所1978-2010年知识产出
通讯作者Chen, H , Tsing Hua Univ, Ctr Adv Study, Beijing 100084, Peoples R China.
推荐引用方式
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):-.

入库方式: OAI收割

来源:理论物理研究所

浏览0
下载0
收藏0
其他版本

除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。