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Importance of Translational Entropy of Water in Biological Self-Assembly Processes like Protein Folding

We briefly review our studies on the folding/unfolding mechanisms of proteins. In biological self-assembly processes such as protein folding, the number of accessible translational configurations of water in the system increases greatly, leading to a large gain in the water entropy. The usual view l...

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Detalles Bibliográficos
Autor principal: Kinoshita, Masahiro
Formato: Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International (MDPI) 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2672019/
https://www.ncbi.nlm.nih.gov/pubmed/19399238
http://dx.doi.org/10.3390/ijms10031064
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author Kinoshita, Masahiro
author_facet Kinoshita, Masahiro
author_sort Kinoshita, Masahiro
collection PubMed
description We briefly review our studies on the folding/unfolding mechanisms of proteins. In biological self-assembly processes such as protein folding, the number of accessible translational configurations of water in the system increases greatly, leading to a large gain in the water entropy. The usual view looking at only the water in the close vicinity of the protein surface is capable of elucidating neither the large entropic gain upon apoplastocyanin folding, which has recently been found in a novel experimental study, nor the pressure and cold denaturation. With the emphasis on the translational entropy of water, we are presently constructing a reliable method for predicting the native structure of a protein from its amino-acid sequence.
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spelling pubmed-26720192009-04-27 Importance of Translational Entropy of Water in Biological Self-Assembly Processes like Protein Folding Kinoshita, Masahiro Int J Mol Sci Review We briefly review our studies on the folding/unfolding mechanisms of proteins. In biological self-assembly processes such as protein folding, the number of accessible translational configurations of water in the system increases greatly, leading to a large gain in the water entropy. The usual view looking at only the water in the close vicinity of the protein surface is capable of elucidating neither the large entropic gain upon apoplastocyanin folding, which has recently been found in a novel experimental study, nor the pressure and cold denaturation. With the emphasis on the translational entropy of water, we are presently constructing a reliable method for predicting the native structure of a protein from its amino-acid sequence. Molecular Diversity Preservation International (MDPI) 2009-03-11 /pmc/articles/PMC2672019/ /pubmed/19399238 http://dx.doi.org/10.3390/ijms10031064 Text en © 2009 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland. This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Review
Kinoshita, Masahiro
Importance of Translational Entropy of Water in Biological Self-Assembly Processes like Protein Folding
title Importance of Translational Entropy of Water in Biological Self-Assembly Processes like Protein Folding
title_full Importance of Translational Entropy of Water in Biological Self-Assembly Processes like Protein Folding
title_fullStr Importance of Translational Entropy of Water in Biological Self-Assembly Processes like Protein Folding
title_full_unstemmed Importance of Translational Entropy of Water in Biological Self-Assembly Processes like Protein Folding
title_short Importance of Translational Entropy of Water in Biological Self-Assembly Processes like Protein Folding
title_sort importance of translational entropy of water in biological self-assembly processes like protein folding
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2672019/
https://www.ncbi.nlm.nih.gov/pubmed/19399238
http://dx.doi.org/10.3390/ijms10031064
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