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Article

Influence of mutations of the N-cap residue, Gly4, on stability and structure of hen lysozyme.

Journal of biochemistry - 1 Jul 1997

Motoshima H, Ueda T, Masumoto K, Hashimoto Y, Chijiiwa Y, Imoto T

Abstract excerpt

Hen lysozyme, with three alpha-helices (A, B, and C), is a c-type lysozyme. In these lysozymes, Ser24 and Asp88 located at the N-cap position in the B- and C-helix, respectively, are mostly conserved, but residue 4 at the N-cap position in A-helix is variable. To investigate the effect of mutatio...

Topics

Amino Acid Sequence
Animals
Binding Sites
Crystallography, X-Ray
Enzyme Stability
Female
Glycine
Guanidine
Guanidines
Hydrogen Bonding
Models, Molecular
Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Muramidase

Mutation

Protein Conformation

Protein Denaturation

Source

Identifiers

PMID: 9276667
DOI: 10.1093/oxfordjournals.jbchem.a021736

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9276667-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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Influence of mutations of the N-cap residue, Gly4, on stability and structure of hen lysozyme.PMID 9276667Read ↗

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