Unfolding proteins in an external field: Can we always observe the intermediate states?

Alexander S. Lemak, James R. Lepock, and Jeff Z. Y. Chen
Phys. Rev. E 67, 031910 – Published 19 March 2003
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Abstract

A protein molecule under the stress of an external denaturing force acting on a terminal end or on the entire molecule is expected to unfold, possibly through a few intermediate stages depending on the magnitude of the denaturing force. We have investigated two protein minimal models under various types of denaturing force fields using the collision molecular-dynamics simulation, in order to critically examine the relationship between the folding pathways observed in different protein denaturing experiments.

  • Received 2 April 2002

DOI:https://doi.org/10.1103/PhysRevE.67.031910

©2003 American Physical Society

Authors & Affiliations

Alexander S. Lemak, James R. Lepock, and Jeff Z. Y. Chen*

  • Department of Physics, University of Waterloo, Waterloo, Ontario, Canada N2L 3G1

  • *Author to whom correspondence should be addressed.

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Vol. 67, Iss. 3 — March 2003

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