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Probing structural and dynamical transitions in polymer globules by force

Charles E. Sing, Thomas R. Einert, Roland R. Netz, and Alfredo Alexander-Katz
Phys. Rev. E 83, 040801(R) – Published 11 April 2011
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Abstract

The dynamics of proteins and biopolymers play a crucial role in their function. By using Brownian dynamics we show that polymer globules, which serve as a model system for proteins, undergo a size-dependent dynamical transition from a liquid-like state at high T to a frozen state at low T with a relaxation time that diverges at the transition point. Furthermore, a stretch-induced melting transition is shown to be readily controlled by external forces that exploit the polymer connectivity to modify the size of the globule. This pathway could be a general route to enhance the rate of conformational changes in naturally occurring biopolymers.

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  • Received 11 January 2011

DOI:https://doi.org/10.1103/PhysRevE.83.040801

©2011 American Physical Society

Authors & Affiliations

Charles E. Sing1, Thomas R. Einert2, Roland R. Netz2, and Alfredo Alexander-Katz1,*

  • 1Department of Material Science, Massachusetts Institute of Technology, 77 Massachusetts Avenue 12-009, Cambridge, Massachusetts 02139, USA
  • 2Physics Department, TU Munich, D-85748 Garching, Germany

  • *aalexand@mit.edu

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Issue

Vol. 83, Iss. 4 — April 2011

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