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Probing structural and dynamical transitions in polymer globules by force

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Author(s)
Sing, Charles E.
•
Einert, Thomas R.
•
Netz, Roland R.
•
Alexander-Katz, Alfredo
Date Issued
April 2011
Journal
Physical Review E
Publisher
American Physical Society
Citation
Sing, Charles et al. “Probing Structural and Dynamical Transitions in Polymer Globules by Force.” Physical Review E 83.4 (2011) ©2011 American Physical Society
Version
Final published version
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.
MIT Department
Massachusetts Institute of Technology. Department of Materials Science and Engineering
Terms of Use
Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.
Persistent DSpace Link
http://hdl.handle.net/1721.1/65552
DOI of Published Version
https://doi.org/10.1103/PhysRevE.83.040801
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