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Lookup NU author(s): Dr Milan Mijajlovic
This is the authors' accepted manuscript of an article that has been published in its final definitive form by American Chemical Society, 2017.
For re-use rights please refer to the publisher's terms and conditions.
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.
Author(s): Ross-Naylor JA, Mijajlovic M, Zhang H, Biggs MJ
Publication type: Article
Publication status: Published
Journal: The Journal of Physical Chemistry B
Year: 2017
Volume: 121
Issue: 51
Pages: 11455-11464
Print publication date: 28/12/2017
Online publication date: 06/12/2017
Acceptance date: 06/12/2017
Date deposited: 21/12/2017
ISSN (print): 1520-6106
ISSN (electronic): 1520-5207
Publisher: American Chemical Society
URL: https://doi.org/10.1021/acs.jpcb.7b10319
DOI: 10.1021/acs.jpcb.7b10319
Notes: The paper is an outcome of a research project on which I was the second supervisor to a PhD student during my postdoctoral appointment in Adelaide.
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