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Article

Polar mutations in membrane proteins as a biophysical basis for disease.

Biopolymers - 1 Jan 2002

Partridge Anthony W, Therien Alex G, Deber Charles M

Abstract excerpt

Transmembrane (TM) alpha-helices are surrounded by the hydrocarbon chains of the lipid bilayer. The low dielectric constant of this environment makes it extremely unfavorable for a residue with a polar side chain to exist in a non-H-bonded state. Therefore, in combination with a wild-type polar residue partner, a polar TM mutant could generate, in some cases, a non-native H-bond that could impair native protein...

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Identifiers

PMID: 12539263
DOI: 10.1002/bip.10313

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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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