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Article

NMR investigation of the dynamics of tryptophan side-chains in hemoglobins.

Journal of molecular biology - 30 Aug 2002

Yuan Yue, Simplaceanu Virgil, Lukin Jonathan A, Ho Chien

Abstract excerpt

NMR relaxation measurements of 15N spin-lattice relaxation rate (R(1)), spin-spin relaxation rate (R(2)), and heteronuclear nuclear Overhauser effect (NOE) have been carried out at 11.7T and 14.1T as a function of temperature for the side-chains of the tryptophan residues of 15N-labeled and/or (2H,15N)-labeled recombinant human normal adult hemoglobin (Hb A) and three recombinant mutant hemoglobins, rHb Kempsey...

Topics

Amino Acid Substitution
Animals
Carbon Monoxide
Hemoglobins
Mutation
Nuclear Magnetic Resonance, Biomolecular
Phytic Acid
Protein Conformation
Recombinant Proteins
Structure-Activity Relationship
Tryptophan

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Identifiers

PMID: 12206767
DOI: 10.1016/s0022-2836(02)00704-0

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-12206767-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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