Pathways of mechanical unfolding of FnIII10: Low force intermediates

被引：12

作者：

Caraglio, M. ^{[1
,2
,3
]}

Imparato, A. ^{[4
]}

Pelizzola, A. ^{[1
,2
,3
]}

机构：

[1] Politecn Torino, Dipartimento Fis, I-10129 Turin, Italy

[2] Ist Nazl Fis Nucl, Sez Torino, I-10125 Turin, Italy

[3] Politecn Torino, CNISM, I-10129 Turin, Italy

[4] Univ Aarhus, Dept Phys & Astron, DK-8000 Aarhus C, Denmark

来源：

JOURNAL OF CHEMICAL PHYSICS | 2010年 / 133卷 / 06期

关键词：

Ising model; molecular biophysics; polymers; stochastic processes; PROTEIN CONFORMATION; MOLECULAR-DYNAMICS; ADHESION BONDS; III MODULE; FIBRONECTIN; SPECTROSCOPY; MODEL; STRENGTH; KINETICS; DOMAINS;

D O I：

10.1063/1.3464476

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

We study the mechanical unfolding pathways of the FnIII(10) domain of fibronectin by means of an Ising-like model, using both constant force and constant velocity protocols. At high forces and high velocities our results are consistent with experiments and previous computational studies. Moreover, the simplicity of the model allows us to probe the biologically relevant low force regime, where we predict the existence of two intermediates with very close elongations. The unfolding pathway is characterized by stochastic transitions between these two intermediates. (C) 2010 American Institute of Physics. [doi:10.1063/1.3464476]

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页数：9

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