A possible allosteric communication pathway identified through a resonance Raman study of four beta37 mutants of human hemoglobin A.

doi:10.1021/bi9708693

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Article

A possible allosteric communication pathway identified through a resonance Raman study of four beta37 mutants of human hemoglobin A.

Biochemistry - 31 Mar 1998

Peterson E S, Friedman J M

Abstract excerpt

The highly conserved tryptophan at position beta37 occupies a key locus at the hinge region within the alpha1beta2 interface of the mammalian hemoglobins. This residue is thought to play an important role in mediating the heme-heme interaction associated with the cooperative binding of oxygen; ho...

Topics

Allosteric Regulation
Amino Acid Substitution
Carbon Monoxide
Heme
Hemoglobin A
Humans
Hydrogen Bonding
Mutation
Oxygen
Photolysis
Protein Binding
Protein Conformation
Protein Structure, Tertiary
Recombinant Proteins
Spectrum Analysis, Raman

Source

Open in PubMed

Identifiers

PMID: 9521755
DOI: 10.1021/bi9708693

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9521755-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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

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