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Article

Characteristic of aromatic amino acid substitution at alpha 96 of hemoglobin.

Journal of biochemistry and molecular biology - 31 Jan 2005

Choi Jong-Whan, Lee Jong Hyuk, Lee Kwang Ho, Lee Hyean-Woo, Sohn Joon Hyung, Yoon Joon Ho, Yeh Byung-Il, Park Seung Kyu, Lee Kyu Jae, Kim Hyun-Won

Abstract excerpt

Replacement of valine by tryptophan or tyrosine at position alpha96 of the alpha chain (alpha96Val), located in the alpha(1)beta(2) subunit interface of hemoglobin leads to low oxygen affinity hemoglobin, and has been suggested to be due to the extra stability introduced by an aromatic amino acid at the alpha96 position. The characteristic of aromatic amino acid substitution at the alpha96 of hemoglobin has been...

Topics

Amino Acid Substitution
Hemoglobins
Humans
Hydrogen Bonding
Magnetic Resonance Spectroscopy
Mutation
Oxygen
Phenylalanine
Protein Subunits
Recombinant Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Tryptophan

Tyrosine

Valine

Source

Identifiers

PMID: 15715956
DOI: 10.5483/bmbrep.2005.38.1.115

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-15715956-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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