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Article

Polar residues in membrane domains of proteins: molecular basis for helix-helix association in a mutant CFTR transmembrane segment.

Biochemistry - 19 Mar 2002

Partridge Anthony W, Melnyk Roman A, Deber Charles M

Abstract excerpt

Polar side chains constitute over 20% of residues in the transmembrane (TM) helices of membrane proteins, where they may serve as hydrogen bond interaction sites for phenotypic polar mutations that arise in membrane protein-related diseases. To systematically explore the structural consequences of H-bonds between TM helices, we focused on TM4 of the cystic fibrosis conductance regulator (CFTR) and its cystic...

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Share to Cystic Fibrosis Transmembrane Conductance Regulator
Share to Electrophoresis, Polyacrylamide Gel

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Protein Binding

Share to Protein Structure, Secondary

Share to Sequence Homology, Amino Acid

Source

Identifiers

PMID: 11888281
DOI: 10.1021/bi0120502

Genes

CFTR
SDS

Variants

Provenance

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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