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Atomic refinement with correlated solid-state NMR restraints.

Richard Bertram1, Tom Asbury, Felcy Fabiola

  • 1Department of Mathematics, Florida State University, Tallahassee, FL 32306-4510, USA. bertram@sb.fsu.edu

Journal of Magnetic Resonance (San Diego, Calif. : 1997)
|August 14, 2003
PubMed
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Correlating solid-state NMR data, specifically dipolar coupling and chemical shift measurements, resolves sign degeneracies. This leads to more accurate atomic structures for membrane proteins during refinement.

Area of Science:

  • Structural biology
  • Biophysical chemistry
  • Solid-state Nuclear Magnetic Resonance (NMR) spectroscopy

Background:

  • Solid-state NMR provides crucial structural insights into membrane proteins.
  • Sign degeneracies in dipolar coupling tensor measurements limit the precision of structural information.
  • Existing atomic refinement methods struggle with these degeneracies, impacting accuracy.

Purpose of the Study:

  • To investigate methods for resolving sign degeneracies in solid-state NMR data.
  • To improve the accuracy of atomic structures determined for membrane proteins.
  • To demonstrate the benefits of correlating multiple NMR data types for refinement.

Main Methods:

  • Simulated solid-state NMR data generation using back-calculation from known membrane protein crystal structures.

Related Experiment Videos

  • Correlation of anisotropic dipolar coupling and anisotropic chemical shift measurements.
  • Atomic refinement of membrane protein structures using correlated NMR data.

    • Main Results:

    • Correlating anisotropic dipolar coupling and chemical shift measurements significantly resolves dipolar sign degeneracies.
    • Utilizing three correlated data types can completely resolve all sign degeneracies.
    • Atomic refinement with correlated data yields structures closer to the original conformations and with a higher proportion of correct dipolar signs.

    Conclusions:

    • Correlating multiple solid-state NMR data types, such as dipolar couplings and chemical shifts, is essential for overcoming sign degeneracies.
    • This approach substantially improves the accuracy and reliability of atomic structures determined for membrane proteins.
    • The developed methodology and software (CNS-SS02) facilitate enhanced structural determination of membrane proteins.