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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Detalles Bibliográficos
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
Descripción
Sumario: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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