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[Dynamics of protein structures].

G Wagner, K Wüthrich

    Die Naturwissenschaften
    |March 1, 1983
    PubMed
    Summary
    This summary is machine-generated.

    This review explores methods for characterizing protein molecule internal mobility, focusing on nuclear magnetic resonance techniques for non-crystalline proteins and their link to biological functions.

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    Area of Science:

    • Biophysics
    • Structural Biology
    • Biochemistry

    Context:

    • Protein molecules exhibit complex internal dynamics crucial for their biological functions.
    • Understanding protein mobility requires advanced experimental and theoretical characterization methods.
    • Non-crystalline protein samples present unique challenges for studying internal dynamics.

    Purpose:

    • To survey and present experimental and theoretical methods for characterizing protein internal mobility.
    • To emphasize the application of high-resolution nuclear magnetic resonance (NMR) spectroscopy.
    • To discuss the correlation between protein dynamics and biological functions.

    Summary:

    • This review details various methods for multi-parameter characterization of protein internal mobility.

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  • High-resolution nuclear magnetic resonance (NMR) is highlighted for its utility in studying non-crystalline proteins.
  • The review explores potential links between the dynamic behavior of proteins and their biological roles.
  • Impact:

    • Provides a comprehensive overview of techniques for assessing protein dynamics.
    • Highlights the importance of NMR spectroscopy in studying challenging protein systems.
    • Facilitates a deeper understanding of how protein motion influences biological activity.