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Application of the Generalized Kinetic Ising Model to the Kinetics of Protein Folding
Author(s) -
Liang Kuo Kan,
Hayashi Michitoshi,
Shiu Ying Jen,
Mo Yan,
Shao Jiushu,
Yan Yijing,
Lin Sheng Hsien
Publication year - 2003
Publication title -
journal of the chinese chemical society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.329
H-Index - 45
eISSN - 2192-6549
pISSN - 0009-4536
DOI - 10.1002/jccs.200300050
Subject(s) - chemistry , kinetics , protein folding , folding (dsp implementation) , thermodynamics , kinetic energy , ising model , statistical physics , classical mechanics , physics , biochemistry , electrical engineering , engineering
The kinetic Ising model in the mean field approximation has been applied to study the equilibrium and kinetic behaviors of protein folding‐unfolding. Thermodynamics and kinetics of protein folding‐unfolding are related by an elementary process of folding ↔ unfolding of peptide bonds. As a demonstration, we analyze, using the presented theory, the equilibrium and kinetics properties of Leu94Val mutant of horse cyt. c (Biochemistry 35 , 5538 (1996).) and several characteristic properties are deduced using our theoretical model.