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Structural dynamics of liganded myoglobin

H Frauenfelder, G A Petsko

    Biophysical Journal
    |October 1, 1980
    PubMed
    Summary
    This summary is machine-generated.

    X-ray crystallography and Mössbauer spectroscopy reveal protein atomic motion. Temperature dependence separates conformational changes from vibrations, showing myoglobin

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    Area of Science:

    • Structural biology
    • Biophysics
    • Protein dynamics

    Background:

    • X-ray crystallography provides atomic-level structural data.
    • Spectroscopic techniques like nuclear magnetic resonance offer temporal information.
    • Understanding atomic motion is crucial for protein function.

    Purpose of the Study:

    • To characterize atomic displacements in sperm whale myoglobin using X-ray crystallography.
    • To differentiate between thermal vibrations and large conformational motions.
    • To investigate the influence of crystal lattice disorder on atomic displacement measurements.

    Main Methods:

    • High-resolution X-ray diffraction data analysis.
    • Mössbauer spectroscopy to estimate crystal lattice disorder contributions.

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  • Temperature dependence studies of mean-square displacements.

    • Main Results:

    • Identified regions of significant conformational motion in myoglobin, especially at chain termini and near the proximal histidine.
    • Observed that mean-square displacement generally increases with distance from the molecule's center of gravity.
    • Found that certain heme pocket regions in oxy cobalt myoglobin are more rigid than in Met myoglobin.

    Conclusions:

    • Combined crystallographic and spectroscopic methods effectively characterize protein dynamics.
    • Distinguishes between thermal vibrations and functionally relevant conformational changes.
    • Myoglobin exhibits distinct dynamic properties in different forms and locations within the molecule.