Cooperativity in Thermal and Force-Induced Protein Unfolding: Integration of Crack Propagation and Network Elasticity Models

被引：28

作者：

Srivastava, Amit ^{[1
]}

Granek, Rony ^{[1
,2
]}

机构：

[1] Ben Gurion Univ Negev, Stella & Avram Goren Goldstein Dept Biotechnol En, IL-84105 Beer Sheva, Israel

[2] Ben Gurion Univ Negev, Ilse Katz Inst Meso & Nanoscale Sci & Technol, IL-84105 Beer Sheva, Israel

来源：

PHYSICAL REVIEW LETTERS | 2013年 / 110卷 / 13期

关键词：

MOLECULAR-DYNAMICS SIMULATIONS; MONTE-CARLO-SIMULATION; TRANSITION-STATE; CHYMOTRYPSIN INHIBITOR-2; SINGLE-MOLECULE; FOLDING PROTEINS; DENATURED STATE; BARNASE; PATHWAY; FLUCTUATIONS;

D O I：

10.1103/PhysRevLett.110.138101

中图分类号：

O4 [物理学];

学科分类号：

0702 ;

摘要：

We investigate force-induced and temperature-induced unfolding of proteins using the combination of a Gaussian network model and a crack propagation model based on "bond''-breaking independent events. We assume the existence of threshold values for the mean strain and strain fluctuations that dictate bond rupture. Surprisingly, we find that this stepwise process usually leads to a few cooperative, first-order-like, transitions in which several bonds break simultaneously, reminiscent of the "avalanches'' seen in disordered networks. DOI: 10.1103/PhysRevLett.110.138101

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页数：5

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