Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Comparison of helix stability in wild-type and mutant LamB signal sequences.

The Journal of biological chemistry - 5 Mar 1990

Bruch M D, Gierasch L M

Abstract excerpt

Previous studies of isolated peptides corresponding to the wild-type signal sequence of the LamB protein of Escherichia coli and to several export-impaired mutants demonstrated that a high tendency to adopt an alpha-helical conformation in low dielectric environments was a property of functional sequences. We have now used nuclear magnetic resonance to establish further characteristics of the helical conformation...

Topics

Amino Acid Sequence
Bacterial Outer Membrane Proteins
Circular Dichroism
Escherichia coli
Magnetic Resonance Spectroscopy
Molecular Sequence Data
Mutation
Peptides
Porins
Protein Conformation
Protein Sorting Signals

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Receptors, Virus

Source

Identifiers

PMID: 2406265

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2406265-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Comparison of helix stability in wild-type and mutant LamB signal sequences.PMID 2406265Read ↗

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

Fluorescence analysis of tryptophan-containing variants of the LamB signal sequence upon insertion into a lipid bilayer.Semantic proximity Read ↗

Structural studies on peptides corresponding to mutants of the major alpha-helix of barnase.Semantic proximity Read ↗

Signal sequence mutations as tools for the characterization of LamB folding intermediates.Semantic proximity Read ↗

Modulation of the structural integrity of helix F in apomyoglobin by single amino acid replacements.Semantic proximity Read ↗

A peptide corresponding to an export-defective mutant OmpA signal sequence with asparagine in the hydrophobic core is unable to insert into model membranes.Semantic proximity Read ↗

Structure and stability of variants of the sarcin-ricin loop of 28S rRNA: NMR studies of the prokaryotic SRL and a functional mutant.Semantic proximity Read ↗

NMR structure of the noncytotoxic alpha-sarcin mutant Delta(7-22): the importance of the native conformation of peripheral loops for activity.Semantic proximity Read ↗

Interaction of wild-type signal sequences and their charged variants with model and natural membranes.Semantic proximity Read ↗

Positional dependence of non-native polar mutations on folding of CFTR helical hairpins.Semantic proximity Read ↗

A mutational study of transmembrane helix-helix interactions.Semantic proximity Read ↗

A single-residue deletion alters the lipid selectivity of a K+ channel-associated peptide in the beta-conformation: spin label electron spin resonance studies.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.