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Article

Protein stability and electrostatic interactions between solvent exposed charged side chains.

Proteins - 1 Jan 1990

Akke M, Forsén S

Abstract excerpt

To investigate the contribution to protein stability of electrostatic interactions between charged surface residues, we have studied the effect of substituting three negatively charged solvent exposed residues with their side-chain amide analogs in bovine calbindin D9k--a small (Mr 8,500) globular protein of the calmodulin superfamily. The free energy of urea-induced unfolding for the wild-type and seven mutant...

Topics

Apoproteins
Calbindins
Escherichia coli
Models, Molecular
Mutation
Protein Conformation
Protein Denaturation
S100 Calcium Binding Protein G
Thermodynamics

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 2217161
DOI: 10.1002/prot.340080106

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2217161-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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