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Article

Estimating the contribution of engineered surface electrostatic interactions to protein stability by using double-mutant cycles.

Biochemistry - 9 Oct 1990

Serrano L, Horovitz A, Avron B, Bycroft M, Fersht A R

Abstract excerpt

Coulombic interactions between charges on the surface of proteins contribute to stability. It is difficult, however, to estimate their importance by protein engineering methods because mutation of one residue in an ion pair alters the energetics of many interactions in addition to the coulombic energy between the two components. We have estimated the interaction energy between two charged residues, Asp-12 and...

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Identifiers

PMID: 2248951
DOI: 10.1021/bi00492a006

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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