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Article

Stability of myoglobin: a model for the folding of heme proteins.

Biochemistry - 4 Oct 1994

Hargrove M S, Krzywda S, Wilkinson A J, Dou Y, Ikeda-Saito M, Olson J S

Abstract excerpt

Factors governing the stability of sperm whale, pig, and human metmyoglobin were examined by (1) measuring guanidinium chloride induced unfolding of apoglobins containing 22 replacements at positions 29(B10), 43(CD1), 64(E7), 68(E11), and 107(G8), (2) determining the rates of hemin loss from the recombinant holoproteins, and (3) estimating constitutive expression levels of the corresponding genes in Escherichia...

Topics

Animals
Apoproteins
Escherichia coli
Heme
Hemeproteins
Humans
Metmyoglobin
Models, Chemical
Models, Molecular
Mutation
Myoglobin
Protein Folding

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Recombinant Proteins

Sequence Homology, Amino Acid

Spectrophotometry, Ultraviolet

Swine

Whales

Source

Identifiers

PMID: 7918393
DOI: 10.1021/bi00205a012

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7918393-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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