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Type: Journal article
Title: Characterizing the switching transitions of an adsorbed peptide by mapping the potential energy surface
Author: Ross-Naylor, J.
Mijajlovic, M.
Zhang, H.
Biggs, M.
Citation: Journal of Physical Chemistry B, 2017; 121(51):11455-11464
Publisher: American Chemical Society
Issue Date: 2017
ISSN: 1520-6106
Statement of
James A. Ross-Naylor, Milan Mijajlovic, Hu Zhang and Mark J. Biggs
Abstract: Peptide adsorption occurs across technology, medicine, and nature. The functions of adsorbed peptides are related to their conformation. In the past, molecular simulation methods such as molecular dynamics have been used to determine key conformations of adsorbed peptides. However, the transitions between these conformations often occur too slowly to be modeled reliably by such methods. This means such transitions are less well understood. In the study reported here, discrete path sampling is used for the first time to study the potential energy surface of an adsorbed peptide (polyalanine) and the transition pathways between various stable adsorbed conformations that have been identified in prior work by two of the authors [ Mijajlovic , M. ; Biggs , M. J. J. Phys. Chem. C 2007 , 111 , 15839 - 15847 ]. Mechanisms for the switching of adsorbed polyalanine between the stable conformations are elucidated along with the energetics of these switches.
Keywords: Peptides; Adsorption; Surface Properties; Molecular Dynamics Simulation
Rights: © 2017 American Chemical Society
RMID: 0030079383
DOI: 10.1021/acs.jpcb.7b10319
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Appears in Collections:Chemical Engineering publications

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