Thermodynamics of Aggregation of Two Proteins(Cross-disciplinary physics and related areas of science and technology)
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概要
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We investigate aggregation mechanism of two proteins in a thermodynamically unambiguous manner by considering the finite size effect of free energy landscape of HP lattice protein model. Multi-self-overlap-ensemble Monte Carlo method is used for numerical calculations. We find that a dimer can be formed spontaneously as a thermodynamically stable state when the system is small enough. It implies the possibility that the aggregation of proteins in a cell is triggered when they are confined in a small region by, for example, being surrounded by other macromolecules. We also find that the dimer exhibits a transition between unstable state and metastable state in the infinite system.
- 社団法人日本物理学会の論文
- 2006-06-15
著者
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Kikuchi Macoto
Cybermedia Center Osaka University
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Kikuchi Macoto
Cybermedia Center Osaka Univ.
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Nakanishi Kazuki
Dep. Of Chemistry Graduate School Of Sci. Kyoto Univ.
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Nakanishi Kazuki
Department Of Chemistry Graduate School Of Science Kyoto University
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