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Assignment of resonances in the h-1 nuclear-magnetic-resonance spectrum of the carbon-monoxide complex of human-hemoglobin alpha-chains

Academic Article
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Overview

authors

  • Dalvit, C.
  • Wright, Peter

publication date

  • March 1987

journal

  • Journal of Molecular Biology  Journal

abstract

  • Assignments are reported for a substantial number of heme and amino acid proton resonances in the 1H nuclear magnetic resonance spectrum of the carbon monoxide complex of isolated hemoglobin alpha-chains. These resonances provide information on the solution conformation of the protein, particularly in the vicinity of the heme. The heme pocket structure is generally similar to that of carbonmonoxymyoglobin; several conserved residues adopt virtually identical positions relative to the heme in the two proteins. The largest conformational differences involve residues surrounding the ligand-binding site, notably Val62 (E11) and His58 (E7). The chemical shifts of the proximal His87 (F8) resonances are very similar in spectra of the two proteins, indicating a highly conserved coordination geometry and similar hydrogen bonding to the backbone carbonyl of Leu83 (F4).

subject areas

  • Amino Acid Sequence
  • Carboxyhemoglobin
  • Heme
  • Hemoglobin A
  • Humans
  • Hydrogen-Ion Concentration
  • Magnetic Resonance Spectroscopy
  • Protons
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Identity

International Standard Serial Number (ISSN)

  • 0022-2836

Digital Object Identifier (DOI)

  • 10.1016/0022-2836(87)90379-2

PubMed ID

  • 3039152
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Additional Document Info

start page

  • 329

end page

  • 339

volume

  • 194

issue

  • 2

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