Composition Preference of Amino Acids in Model-Proteins
WANG Jian-Yong, WANG Jun, WANG Wei
National Laboratory of Solid State Microstructure and Department of Physics, Nanjing University, Nanjing 210093
Composition Preference of Amino Acids in Model-Proteins
WANG Jian-Yong;WANG Jun;WANG Wei
National Laboratory of Solid State Microstructure and Department of Physics, Nanjing University, Nanjing 210093
关键词 ：
87.15.Cc ,
87.15.Aa ,
87.14.Ee
Abstract ： The folding behaviour of some sequences of 36 monomers with different proportion of hydrophobic residues in a three-dimensional lattice based on the Miyazawa-Jernigen interaction matrix. It is found that the sequences with good folding properties are those with an optimal number of hydrophobic residues, neither too many nor too few. The reason for the deterioration of folding properties of sequences out of this range has also been analysed.
Key words ：
87.15.Cc
87.15.Aa
87.14.Ee
出版日期: 2001-03-01
引用本文:
WANG Jian-Yong;WANG Jun;WANG Wei. Composition Preference of Amino Acids in Model-Proteins[J]. 中国物理快报, 2001, 18(3): 449-451.
链接本文:
https://cpl.iphy.ac.cn/CN/
或
https://cpl.iphy.ac.cn/CN/Y2001/V18/I3/449
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