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Article

Structures of wild-type and mutant signal sequences of Escherichia coli ribose binding protein.

Biophysical journal - 1 May 1994

Yi G S, Choi B S, Kim H

Abstract excerpt

The structure of a chemically synthesized 25-residue-long functional signal peptide of Escherichia coli ribose binding protein was compared with that of a nonfunctional mutant-signal peptide using circular dichroism and two-dimensional 1H NMR in solvents mimicking the amphiphilic environments. The functional peptide forms an 18-residue-long alpha-helix starting from the NH2-terminal region and reaching to the...

Topics

Amino Acid Sequence
Carrier Proteins
Circular Dichroism
Escherichia coli
Escherichia coli Proteins
Magnetic Resonance Spectroscopy
Molecular Sequence Data
Molecular Structure
Mutation
Periplasmic Binding Proteins
Protein Sorting Signals

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Ribose

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Identifiers

PMID: 8061209
DOI: 10.1016/S0006-3495(94)80952-X
PMCID: PMC1275880

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-8061209-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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