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Article

Hydrophobic content and lipid interactions of wild-type and mutant OmpA signal peptides correlate with their in vivo function.

Biochemistry - 22 Oct 1991

Hoyt D W, Gierasch L M

Abstract excerpt

Peptides corresponding to the wild-type signal sequence of the Escherichia coli outer membrane protein OmpA and several mutants have been synthesized and characterized biophysically. The mutations were designed collaboratively with Inouye and co-workers to test the understanding of the critical characteristics of signal sequences required for their functions. The in vivo results for these mutants have been...

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Identifiers

PMID: 1931946
DOI: 10.1021/bi00106a012

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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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Hydrophobic content and lipid interactions of wild-type and mutant OmpA signal peptides correlate with their in vivo function.PMID 1931946Read ↗

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