Stretching of proteins in the entropic limit

Marek Cieplak, Trinh Xuan Hoang, and Mark O. Robbins
Phys. Rev. E 69, 011912 – Published 30 January 2004
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Abstract

Mechanical stretching of six proteins is studied through molecular dynamics simulations. The model is Go-like, with Lennard-Jones interactions at native contacts. Low-temperature unfolding scenarios are remarkably complex and sensitive to small structural changes. Thermal fluctuations reduce the peak forces and the number of metastable states during unfolding. The unfolding pathways also simplify as temperature rises. In the entropic limit, all proteins show a monotonic decrease of the extension where bonds rupture with their separation along the backbone (contact order).

  • Received 11 April 2003

DOI:https://doi.org/10.1103/PhysRevE.69.011912

©2004 American Physical Society

Authors & Affiliations

Marek Cieplak1,2, Trinh Xuan Hoang3, and Mark O. Robbins1

  • 1Department of Physics and Astronomy, The Johns Hopkins University, Baltimore, Maryland 21218, USA
  • 2Institute of Physics, Polish Academy of Sciences, Aleja Lotników 32/46, 02-668 Warsaw, Poland
  • 3The Abdus Salam International Center for Theoretical Physics, Strada Costiera 11, 34014 Trieste, Italy

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Vol. 69, Iss. 1 — January 2004

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