ArticleBioinformation2019
Stability of buried and networked salt-bridges (BNSB)in thermophilic proteins.
Article in Bioinformation, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Biophysical and Computational Approaches to Unravel pH-Dependent Conformational Change of PspA Assist PspA-PspF Complex Formation in Yersinia enterocolitica.The protein journal · 2022Article
- Intrinsic basis of thermostability of prolyl oligopeptidase from Pyrococcus furiosus.Scientific reports · 2021Article
- Article
- Salt-bridges in the microenvironment of stable protein structures.Bioinformation · 2020Article
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Authors and funding
5 authors.
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Abstract
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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