Effect of hydrogen bond interaction on protein phase transition

Effect of hydrogen bond interaction on protein phase transition

We derive the grand partition function of protein chain by restricting dihedral angles to exist only in five distinct states and assume that the dominant noncovalent potential is the hydrogen bond interaction. We investigate the phase transition of protein secondary structures and the order of the t...

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Main Authors: Leong, Hon Wai, Chew, Lock Yue
Other Authors: School of Physical and Mathematical Sciences
Format: Article
Language:English
Published: 2013
Subjects:
DRNTU::Science::Biological sciences::Biochemistry
Online Access:https://hdl.handle.net/10356/95441
http://hdl.handle.net/10220/9239
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Institution: Nanyang Technological University
Language: English
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spelling sg-ntu-dr.10356-954412023-02-28T19:37:46Z Effect of hydrogen bond interaction on protein phase transition Leong, Hon Wai Chew, Lock Yue School of Physical and Mathematical Sciences High Performance Computing Centre DRNTU::Science::Biological sciences::Biochemistry We derive the grand partition function of protein chain by restricting dihedral angles to exist only in five distinct states and assume that the dominant noncovalent potential is the hydrogen bond interaction. We investigate the phase transition of protein secondary structures and the order of the transition through analyzing its heat capacity. Our theory demonstrates the presence of α-β-coil structural phase transition in the protein polyalanine. Published version 2013-02-25T04:46:00Z 2019-12-06T19:14:56Z 2013-02-25T04:46:00Z 2019-12-06T19:14:56Z 2012 2012 Journal Article Leong, H. W., & Chew, L. Y. (2012). Effect of hydrogen bond interaction on protein phase transition. Physical review E, 86(3), 031902-. https://hdl.handle.net/10356/95441 http://hdl.handle.net/10220/9239 10.1103/PhysRevE.86.031902 en Physical review E © 2012 American Physical Society. This paper was published in Physical Review E and is made available as an electronic reprint (preprint) with permission of American Physical Society. The paper can be found at the following official DOI: [http://dx.doi.org/10.1103/PhysRevE.86.031902]. One print or electronic copy may be made for personal use only. Systematic or multiple reproduction, distribution to multiple locations via electronic or other means, duplication of any material in this paper for a fee or for commercial purposes, or modification of the content of the paper is prohibited and is subject to penalties under law. application/pdf
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic DRNTU::Science::Biological sciences::Biochemistry
spellingShingle DRNTU::Science::Biological sciences::Biochemistry
Leong, Hon Wai
Chew, Lock Yue
Effect of hydrogen bond interaction on protein phase transition
description We derive the grand partition function of protein chain by restricting dihedral angles to exist only in five distinct states and assume that the dominant noncovalent potential is the hydrogen bond interaction. We investigate the phase transition of protein secondary structures and the order of the transition through analyzing its heat capacity. Our theory demonstrates the presence of α-β-coil structural phase transition in the protein polyalanine.
author2 School of Physical and Mathematical Sciences
author_facet School of Physical and Mathematical Sciences
Leong, Hon Wai
Chew, Lock Yue
format Article
author Leong, Hon Wai
Chew, Lock Yue
author_sort Leong, Hon Wai
title Effect of hydrogen bond interaction on protein phase transition
title_short Effect of hydrogen bond interaction on protein phase transition
title_full Effect of hydrogen bond interaction on protein phase transition
title_fullStr Effect of hydrogen bond interaction on protein phase transition
title_full_unstemmed Effect of hydrogen bond interaction on protein phase transition
title_sort effect of hydrogen bond interaction on protein phase transition
publishDate 2013
url https://hdl.handle.net/10356/95441
http://hdl.handle.net/10220/9239
_version_ 1759857888721895424

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