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题名: Secondary-structure-favored hydrophobic-polar lattice model of protein folding
作者: Chen, H ;  Zhou, X ;  Ou-Yang, ZC
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
学科分类: Physics
通讯作者: Chen, H , Tsing Hua Univ, Ctr Adv Study, Beijing 100084, Peoples R China.
部门归属: Tsing Hua Univ, Ctr Adv Study, Beijing 100084, Peoples R China; Acad Sinica, Inst Theoret Phys, Beijing 100080, Peoples R China
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.
收录类别: SCI
WOS记录号: WOS:000171649000052
Citation statistics: 
内容类型: 期刊论文
URI标识: http://ir.itp.ac.cn/handle/311006/13659
Appears in Collections:理论物理所1978-2010年知识产出_期刊论文

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Recommended Citation:
Chen, H,Zhou, X,Ou-Yang, ZC. Secondary-structure-favored hydrophobic-polar lattice model of protein folding[J]. PHYSICAL REVIEW E,2001,64(4):-.
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