Microscopic mechanism for cold denaturation

被引:114
作者
Dias, Cristiano L. [1 ]
Ala-Nissila, Tapio [2 ,3 ]
Karttunen, Mikko [4 ]
Vattulainen, Ilpo [5 ,6 ,7 ]
Grant, Martin [1 ]
机构
[1] McGill Univ, Dept Phys, Montreal, PQ H3A 2T8, Canada
[2] Brown Univ, Dept Phys, Providence, RI 02912 USA
[3] Aalto Univ, Dept Engn Phys, FI-02015 Espoo, Finland
[4] Univ Western Ontario, Dept Appl Math, London, ON, Canada
[5] Tampere Univ Technol, Inst Phys, FI-33101 Tampere, Finland
[6] Univ So Denmark, Ctr Biomembrane Phys, MEMPHYS, Odense, Denmark
[7] Aalto Univ, Helsinki Inst Phys, Helsinki, Finland
关键词
D O I
10.1103/PhysRevLett.100.118101
中图分类号
O4 [物理学];
学科分类号
0702 ;
摘要
We elucidate the mechanism of cold denaturation through constant-pressure simulations for a model of hydrophobic molecules in an explicit solvent. We find that the temperature dependence of the hydrophobic effect induces, facilitates, and is the driving force for cold denaturation. The physical mechanism underlying this phenomenon is identified as the destabilization of hydrophobic contact in favor of solvent-separated configurations, the same mechanism seen in pressure-induced denaturation. A phenomenological explanation proposed for the mechanism is suggested as being responsible for cold denaturation in real proteins.
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页数:4
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