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Protein conformation from electron spin relaxation data.

J P Allen, J T Colvin, D G Stinson

    Biophysical Journal
    |June 1, 1982
    PubMed
    Summary
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    This study introduces a fractal model to analyze electron spin relaxation in ferric proteins, revealing protein structure via fractal dimension (d). This parameter accurately predicts relaxation rates and conformational changes.

    Area of Science:

    • Biophysics
    • Structural Biology
    • Computational Biology

    Background:

    • Protein structure influences biological function.
    • Electron spin relaxation is sensitive to molecular dynamics and structure.
    • Fractal geometry offers a novel approach to describing complex biological structures.

    Purpose of the Study:

    • To analyze electron spin relaxation data of ferric proteins using a fractal model.
    • To characterize protein structures by a fractal dimension (d).
    • To investigate the relationship between fractal dimension and the temperature dependence of electron spin relaxation rates.

    Main Methods:

    • Analysis of electron spin relaxation data from five ferric proteins.
    • Application of a fractal model to protein structures.

    Related Experiment Videos

  • Computation of fractal dimensions (d) using X-ray diffraction data for 17 proteins.
  • Comparison of fractal dimensions derived from relaxation and X-ray data.

    • Main Results:

    • Protein structures can be characterized by a single parameter, the fractal dimension (d).
    • The fractal dimension (d) determines the temperature dependence of Raman electron spin relaxation rate (T3 + 2d).
    • Fractal dimensions calculated from spin relaxation data closely match those from X-ray data for proteins like ferredoxin and ferricytochrome c.
    • Values of d ranged from 1.34 to 1.76 for the studied proteins.

    Conclusions:

    • The fractal model provides a valid framework for understanding electron spin relaxation in proteins.
    • Fractal dimension (d) is a key structural parameter influencing protein dynamics and relaxation properties.
    • Electron spin resonance spectroscopy, analyzed through this fractal model, can be applied to study protein conformational changes.