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Chemical shifts and three-dimensional protein structures

E Oldfield1

  • 1Department of Chemistry, University of Illinois at Urbana-Champaign 61801, USA.

Journal of Biomolecular NMR
|April 1, 1995
PubMed
Summary

Computing NMR chemical shifts for proteins is now possible, aiding structure determination and refinement. Advances in computational power will expand their use in diverse biological studies.

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Area of Science:

  • Biophysics
  • Computational Chemistry
  • Structural Biology

Background:

  • Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful tool for determining protein structures.
  • Traditionally, NMR chemical shifts were primarily used for assignment verification.
  • Recent advancements enable ab initio computation of NMR chemical shifts for various nuclei (13C, 15N, 19F) in proteins.

Purpose of the Study:

  • To highlight the growing utility of computed NMR chemical shifts as a supplement to established structural determination methods.
  • To explore the potential applications of chemical shift analysis in understanding protein conformation and dynamics.
  • To forecast future developments and broader applications of chemical shift calculations in structural biology.

Main Methods:

  • Ab initio computation of 13C, 15N, and 19F NMR chemical shifts for native proteins.
  • Analysis of chemical shifts to extract information on dihedral angles (phi, psi, chi) and hydrogen-bonding effects.
  • Development and accessibility of shielding hypersurfaces for conformational analysis.

Main Results:

  • Computed NMR chemical shifts provide valuable data for protein structure refinement and prediction.
  • 13C NMR shifts offer insights into torsional angles, aiding assignment verification.
  • 15N shifts reflect torsional and hydrogen-bonding influences, while 19F shifts indicate local charge fields.
  • Shielding hypersurfaces are becoming accessible, linking chemical shifts to molecular conformation.

Conclusions:

  • Computed NMR chemical shifts are emerging as a valuable tool for protein structural characterization.
  • Future improvements in theory and computation will facilitate routine use of chemical shifts in diverse structural studies.
  • Chemical shifts, including non-equivalence due to folding, are increasingly useful for characterizing protein structures and dynamics.

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