Characterization of hydrophobic cores in apomyoglobin: A proton NMR spectroscopy study
- The Pennsylvania State Univ., University Park, PA (USA)
A proton nuclear magnetic resonance spectroscopic study of horse apomyoglobin was undertaken in order to define the regions of myoglobin that are and that are not structurally affected by the binding of the prosthetic group. It was found that, in spite of the poor spectral resolution, a number of spin systems could be identified by using standard correlated methods. Four clusters consisting mostly of hydrophobic residues were detected by nuclear Overhauser spectroscopy, two of which involved the tryptophan side chains. Extensive similarities to nuclear Overhauser spectroscopy data collected on the carbonmonoxy form of holomyoglobin suggested tentative assignments for several residues. It appeared that distinct cores of side chains on the distal side of the binding pocket and between the A, B, G, and H helices maintain the same packing as they do in holomyoglobin and apomyoglobin reconstituted with protoporphyrin IX.
- OSTI ID:
- 5659402
- Journal Information:
- Biochemistry; (USA), Journal Name: Biochemistry; (USA) Vol. 29:50; ISSN 0006-2960; ISSN BICHA
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
62 RADIOLOGY AND NUCLEAR MEDICINE
AMINO ACIDS
ANIMALS
AZOLES
BARYONS
CARBOXYLIC ACIDS
CHEMICAL SHIFT
DRUGS
ELEMENTARY PARTICLES
FERMIONS
GLOBINS
HADRONS
HEAVY WATER
HETEROCYCLIC ACIDS
HETEROCYCLIC COMPOUNDS
HISTIDINE
HORSES
HYDROGEN COMPOUNDS
IMIDAZOLES
LEUCINE
LIPOTROPIC FACTORS
MAGNETIC RESONANCE
MAMMALS
METHIONINE
MYOGLOBIN
NMR SPECTRA
NUCLEAR MAGNETIC RESONANCE
NUCLEONS
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
ORGANIC SULFUR COMPOUNDS
OVERHAUSER EFFECT
OXYGEN COMPOUNDS
PHENYLALANINE
PIGMENTS
PORPHYRINS
PROTEINS
PROTONS
RESONANCE
SPECTRA
VERTEBRATES
WATER