ArticleBioinformation2020
Salt-bridges in the microenvironment of stable protein structures.
Article in Bioinformation, 2020. 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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4 citing papers in PubMed, 11 citations in OpenAlex.
- Local microenvironments of capsomer variants in the PBCV-1.Journal of structural biology · 2025Article
- Molecular Cloning, Optimization of Expression and Functional Characterization of the Global Transcriptional Regulator MosR (Rv0348) of Mycobacterium tuberculosis.Applied biochemistry and biotechnology · 2025Article
- Enhancing recombinant growth factor and serum protein production for cultivated meat manufacturing.Microbial cell factories · 2025Review
- Intrinsic basis of thermostability of prolyl oligopeptidase from Pyrococcus furiosus.Scientific reports · 2021Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
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Abstract
Salt-bridges (sb) play an important role in the folding and stability of proteins. This is deduced from the evaluation of net energy in the microenvironments (ME, residues that are 4 Å away from positive and negative partners of salt-bridge and interact with them). MEs act as a determinant of net-energy due to the intrinsic features in the sequence. The stability of extremophilic proteins is due to the presence of favorable residues at the ME without any unfavorable residues. We studied a dataset of four structures from the protein data bank (PDB) and a homology model (1HM5) to gain insights on this issue. Data shows that the presence of isolated charges and polar residues in the core of extremophilic proteins helps in the formation of stable salt-bridges with reduced desolvation. Thus, site-specific mutations with favorable residues at the ME will help to develop thermo stable proteins with strong salt bridges.
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