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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...

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Source

Identifiers

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

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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