Stability of buried and networked salt-bridges (BNSB)in thermophilic proteins

Thermophilic proteins function at high temperature, unlike mesophilic proteins. Thermo-stability of these proteins is due to the unique buried and networked salt-bridge (BNSB). However, it is known that the desolvation cost of BNSB is too high compared to other favorable energy terms. Nonetheless, i...

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Autores principales: Bandyopadhyay, Amal Kumar, Islam, Rifat Nawaz Ul, Mitra, Debanjan, Banerjee, Sahini, Goswami, Arunava
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Biomedical Informatics 2019
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6651030/
https://www.ncbi.nlm.nih.gov/pubmed/31360001
http://dx.doi.org/10.6026/97320630015061
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author Bandyopadhyay, Amal Kumar
Islam, Rifat Nawaz Ul
Mitra, Debanjan
Banerjee, Sahini
Goswami, Arunava
author_facet Bandyopadhyay, Amal Kumar
Islam, Rifat Nawaz Ul
Mitra, Debanjan
Banerjee, Sahini
Goswami, Arunava
author_sort Bandyopadhyay, Amal Kumar
collection PubMed
description Thermophilic proteins function at high temperature, unlike mesophilic proteins. Thermo-stability of these proteins is due to the unique buried and networked salt-bridge (BNSB). However, it is known that the desolvation cost of BNSB is too high compared to other favorable energy terms. Nonetheless, it is known that stability is provided generally by hydrophobic isosteres without the need for BNSB. We show in this analysis that the BNSB is the optimal evolutionary design of salt-bridge to offset desolvation cost efficiently. Hence, thermophilic proteins with a high level of BNSB provide thermo-stability.
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spelling pubmed-66510302019-07-29 Stability of buried and networked salt-bridges (BNSB)in thermophilic proteins Bandyopadhyay, Amal Kumar Islam, Rifat Nawaz Ul Mitra, Debanjan Banerjee, Sahini Goswami, Arunava Bioinformation Research Article Thermophilic proteins function at high temperature, unlike mesophilic proteins. Thermo-stability of these proteins is due to the unique buried and networked salt-bridge (BNSB). However, it is known that the desolvation cost of BNSB is too high compared to other favorable energy terms. Nonetheless, it is known that stability is provided generally by hydrophobic isosteres without the need for BNSB. We show in this analysis that the BNSB is the optimal evolutionary design of salt-bridge to offset desolvation cost efficiently. Hence, thermophilic proteins with a high level of BNSB provide thermo-stability. Biomedical Informatics 2019-02-03 /pmc/articles/PMC6651030/ /pubmed/31360001 http://dx.doi.org/10.6026/97320630015061 Text en © 2019 Biomedical Informatics http://creativecommons.org/licenses/by/3.0/ This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.
spellingShingle Research Article
Bandyopadhyay, Amal Kumar
Islam, Rifat Nawaz Ul
Mitra, Debanjan
Banerjee, Sahini
Goswami, Arunava
Stability of buried and networked salt-bridges (BNSB)in thermophilic proteins
title Stability of buried and networked salt-bridges (BNSB)in thermophilic proteins
title_full Stability of buried and networked salt-bridges (BNSB)in thermophilic proteins
title_fullStr Stability of buried and networked salt-bridges (BNSB)in thermophilic proteins
title_full_unstemmed Stability of buried and networked salt-bridges (BNSB)in thermophilic proteins
title_short Stability of buried and networked salt-bridges (BNSB)in thermophilic proteins
title_sort stability of buried and networked salt-bridges (bnsb)in thermophilic proteins
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6651030/
https://www.ncbi.nlm.nih.gov/pubmed/31360001
http://dx.doi.org/10.6026/97320630015061
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