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Article

Proline residues in transmembrane alpha helices affect the folding of bacteriorhodopsin.

Journal of molecular biology - 27 Apr 2001

Lu H, Marti T, Booth P J

Abstract excerpt

Proline residues occur frequently in transmembrane alpha helices, which contrasts with their behaviour as helix-breakers in water-soluble proteins. The three membrane-embedded proline residues of bacteriorhodopsin have been replaced individually by alanine and glycine to give P50A, or P50G on helix B, P91A, or P91G on helix C, and P186A or P186G on helix F, and the effect on the protein folding kinetics has been...

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Identifiers

PMID: 11327778
DOI: 10.1006/jmbi.2001.4605

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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