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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/15195
Title: Conformational transitions of a confined lattice protein: A Wang-Landau study
Authors: Busara Pattanasiri
Ying Wai Li
David P. Landau
Thomas Wüst
Wannapong Triampo
The University of Georgia
Mahidol University
Eidgenossische Forschungsanstalt fur Wald, Schnee Und Landschaft Eth-Bereichs
South Carolina Commission on Higher Education
Keywords: Physics and Astronomy
Issue Date: 1-Jan-2012
Citation: Journal of Physics: Conference Series. Vol.402, No.1 (2012)
Abstract: We use Wang-Landau sampling with suitable Monte Carlo trial moves to study a hydrophobic-polar (HP) lattice protein confined between two parallel, attractive walls. The density of states is determined iteratively by a random walk in energy space. Thermodynamic and structural properties, such as specific heat, number of surface contacts and number of H-H monomer pairs, are then calculated. When the surface attraction is comparable to the internal attraction among the hydrophobic monomers in the chain, two conformational "transitions", adsorption at higher temperature and collapse at lower temperature, have been analyzed based on these properties. This transition behavior depends on the variation of surface separation. © Published under licence by IOP Publishing Ltd.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84872575522&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/15195
ISSN: 17426596
17426588
Appears in Collections:Scopus 2011-2015

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