Composition Preference of Amino Acids in Model-Proteins

Chin. Phys. Lett.

2001, Vol. 18

Issue (3): 449-451 DOI:

Original Articles

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

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WANG Jian-Yong, WANG Jun, WANG Wei 2001 Chin. Phys. Lett. 18 449-451

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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.

Keywords: 87.15.Cc 87.15.Aa 87.14.Ee

Published: 01 March 2001

PACS:	87.15.Cc	(Folding: thermodynamics, statistical mechanics, models, and pathways)
	87.15.Aa
	87.14.Ee

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https://cpl.iphy.ac.cn/ OR https://cpl.iphy.ac.cn/Y2001/V18/I3/0449

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