Structural dynamics of liganded myoglobin

Journal Article · Wed Oct 01 00:00:00 EDT 1980 · Biophys. J.; (United States)

DOI:https://doi.org/10.1016/S0006-3495(80)84984-8· OSTI ID:6795861

Frauenfelder, H ^[1]; Petsko, G A

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1. Univ. of Illinois, Urbana

X-ray crystallography can reveal the magnitudes and principal directions of the mean-square displacements of every atom in a protein. This structural information is complementary to the temporal information obtainable by spectroscopic techniques such as nuclear magnetic resonance. Determination of the temperature dependence of the mean-square displacements makes it possible to separate large conformational motions from simple thermal vibrations. The contribution of crystal lattice disorder to the overall apparent displacement can be estimated by Moessbauer spectroscopy. This technique has been applied to high resolution x-ray diffraction data from sperm whale myoglobin in its Met iron and oxy cobalt forms. Both crystal structures display regions of large conformational motions, particularly at the chain termini and in the region of the proximal histidine. Overall, the mean-square displacement increases with increasing distance from the center of gravity of the molecule. Some regions of the heme pocket in oxy cobalt myoglobin are more rigid than the corresponding regions in Met myoglobin.

• OSTI ID: 6795861
• Journal Information: Biophys. J.; (United States), Vol. 32:1
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
MYOGLOBIN
STRUCTURAL CHEMICAL ANALYSIS
HEME
LIGANDS
MICROSTRUCTURE
MOLECULAR STRUCTURE
NMR SPECTRA
TEMPERATURE DEPENDENCE
ULTRASTRUCTURAL CHANGES
X-RAY DIFFRACTION
CARBOXYLIC ACIDS
COHERENT SCATTERING
CRYSTAL STRUCTURE
DIFFRACTION
GLOBIN
HETEROCYCLIC ACIDS
HETEROCYCLIC COMPOUNDS
MORPHOLOGICAL CHANGES
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
PIGMENTS
PORPHYRINS
PROTEINS
SCATTERING
SPECTRA
550200* - Biochemistry
551000 - Physiological Systems