Probing the conformation of hemoglobin presbyterian in the R-state.

doi:10.1023/a:1025080801951

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Article

Probing the conformation of hemoglobin presbyterian in the R-state.

Journal of protein chemistry - 1 Apr 2003

Acharya Seetharama A, Malavalli Ashok, Peterson Eric, Sun Philip D, Ho Chien, Prabhakaran Muthuchidambaram, Arnone Arthur, Manjula Belur N, Friedman Joel M

Abstract excerpt

The influence of allosteric effectors on the R-state (liganded) conformation of Tg-HbP (human hemoglobin Presbyterian expressed in transgenic pig) has been probed using a number of biophysical techniques, and the results have been compared with that of liganded of HbA (human normal adult hemoglobin) to gain insight into the molecular basis of Asn-108(beta)->Lys mutation-induced low-oxygen affinity of Hb. The...

Topics

Allosteric Regulation
Allosteric Site
Animals
Animals, Genetically Modified
Hemoglobin A
Hemoglobins, Abnormal
Humans
Ions
Kinetics
Ligands
Magnetic Resonance Spectroscopy

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Models, Molecular

Mutation

Oxygen

Photochemistry

Protein Structure, Quaternary

Spectrum Analysis, Raman

Swine

Source

Open in PubMed

Identifiers

PMID: 12962322
DOI: 10.1023/a:1025080801951

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-12962322-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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