Statistical Mechanical Theory of Protein Conformation and Its Transition(Cross-disciplinary physics and related areas of science and technology)
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概要
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The statistical mechanical theory of the structural transitions of proteins is developed in accordance with the island model by considering the hydrophobic interactions and the entropy factors while connecting the two hydrophobic residues. The proteins treated here are apo-α-lactalbumin (1B9O), lysozyme (1LZ1), ferrocytochrome c (1CYC), cytochrome c (isozyme 1) (1YCC), chymotrypsin inhibitor 2 (2CI2), and ubiquitin (1UBQ). Among them, according to the experiments, 2CI2 and 1UBQ do not exhibit intermediate structures (two-state model), but others do exhibit intermediate structures that are sometimes termed molten globules (three-state model). The theory related to these facts is given in terms of the island model, specifically 1B9O and 1LZ1. The stability or instability of the intermediate structures is explained by the effects of entropy during folding and the amino acid sequence. The intermediate structure is composed of several stable islands, which become unstable during unfolding.
- 社団法人日本物理学会の論文
- 2007-07-15
著者
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KOBAYASHI Yukio
Department of Medical Oncology, National Cancer Center Hospital
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Wako Hiroshi
School Of Social Science Waseda University
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Wako Hiroshi
School Of Social Sci. Waseda Univ.
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Saito Nobuhiko
Department Of Applied Physics School Of Science And Engineering Waseda University
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Saito Nobuhiko
Department Of Applied Physics Faculty Of Sciencc And Engineering Waseda University
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Kobayashi Yukio
Department Of Information Systems Science Faculty Of Engineering Soka University
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Kobayashi Yukio
Department Of Chemistry Faculity Of Science Tokai University
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Saito Nobuhiko
Department Of Applied Physics And Science And Engineering Research Institute Waseda University
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SAITO Nobuhiko
Department of Applied Physics, School of Science and Engineering, Waseda University
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