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Article

Structure and function of hemoglobin variants at an internal hydrophobic site: consequences of mutations at the beta 27 (B9) position.

Biochemistry - 31 Jul 1990

Huang Y, Pagnier J, Magne P, Baklouti F, Kister J, Delaunay J, Poyart C, Fermi G, Perutz M F

Abstract excerpt

We have studied the structure-function relationships in newly discovered hemoglobin (Hb) mutants with substitutions occurring at the tight and highly hydrophobic cluster between the B and G helices in the beta chains, namely, Hb Knossos or beta A27S and Hb Grange-Blanche or beta A27V. The beta A27S mutant has a 50% decrease in oxygen affinity relative to native human Hb A, while the beta A27V mutant has an...

Topics

Binding Sites
Genetic Variation
Hemoglobins, Abnormal
Humans
Mutation
Oxygen
Protein Conformation
Structure-Activity Relationship
X-Ray Diffraction

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 2223757
DOI: 10.1021/bi00482a010

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2223757-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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