Crystallographic, molecular modeling, and biophysical characterization of the valine beta 67 (E11)-->threonine variant of hemoglobin.

doi:10.1021/bi9519967

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Article

Crystallographic, molecular modeling, and biophysical characterization of the valine beta 67 (E11)-->threonine variant of hemoglobin.

Biochemistry - 13 Feb 1996

Pechik I, Ji X, Fidelis K, Karavitis M, Moult J, Brinigar W S, Fronticelli C, Gilliland G L

Abstract excerpt

The crystal structure of the mutant deoxyhemoglobin in which the beta-globin Val67(E11) has been replaced with threonine [Fronticelli et al. (1993) Biochemistry 32, 1235-1242] has been determined at 2.2 A resolution. Prior to the crystal structure determination, molecular modeling indicated that the Thr67(E11) side chain hydroxyl group in the distal beta-heme pocket forms a hydrogen bond with the backbone...

Topics

Biophysical Phenomena
Biophysics
Carboxyhemoglobin
Crystallography, X-Ray
Electrochemistry
Genetic Variation
Heme
Hemoglobin A
Hemoglobins
Humans
In Vitro Techniques

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Models, Molecular

Nitric Oxide

Oxidation-Reduction

Point Mutation

Protein Conformation

Protein Folding

Protein Processing, Post-Translational

Source

Open in PubMed

Identifiers

PMID: 8639677
DOI: 10.1021/bi9519967

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-8639677-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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