Title

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

Authors

Amal Kumar Bandyopadhyay^*1, Rifat Nawaz Ul Islam^2$, Debanjan Mitra^1$, Sahini Banerjee^3$ & Arunava Goswami³

Affiliation

¹Department of Biotechnology, University of Burdwan, Burdwan, West Bengal, India; ²Department of Zoology, University of Burdwan, Burdwan, West Bengal, India; ³Department of Biological Sciences, ISI, Kolkata, West Bengal, India; $equally contributed

Email

Amal Kumar Bandyopadhyay – E-mail: akbanerjee@biotech.buruniv.ac.in; *Corresponding author

Article Type

Research Article

Date

Received January 21, 2019; Accepted February 2, 2019; Published February 3, 2019

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 favourable 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.

Keywords

Thermophilic protein; stability; networked salt-bridge; buried; desolvation cost; novel method

Citation

Bandyopadhyay et al. Bioinformation 15(1): 61-67 (2019)

Edited by

P Kangueane

ISSN

0973-2063

Publisher

Biomedical Informatics

License

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.