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Article

Crystallographic analysis of mutant human haemoglobins made in Escherichia coli.

Nature - 1 Jan 2000

Luisi B F, Nagai K

Abstract excerpt

The expression of beta-globin in Escherichia coli has enabled us to study the functional role of individual amino-acid residues in haemoglobin (Hb) by site-directed mutagenesis. In contrast to mammalian Hbs, some teleost fish haemoglobins show a drastic lowering of oxygen affinity and cooperativity at low pH, a phenomenon known as the Root effect. We have produced the two mutant haemoglobins Hb Nymphéas...

Topics

Amino Acids
Crystallography
Escherichia coli
Globins
Hemoglobins
Humans
Models, Molecular
Mutation
Structure-Activity Relationship
X-Ray Diffraction

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 3515199
DOI: 10.1038/320555a0

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-3515199-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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