On the origin of residual dipolar couplings from denatured proteins

J Am Chem Soc. 2003 Dec 17;125(50):15647-50. doi: 10.1021/ja035427v.

Abstract

Effects of steric obstruction on random flight chains are examined. Spatial probability distributions are elaborated to calculate residual dipolar couplings and residual chemical shift anisotropy, parameters that are acquired by NMR spectroscopy from solutes dissolved in dilute liquid crystals. Calculations yield chain length and residue position-dependent values in good agreement with simulations to provide understanding of recently acquired data from denatured proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anisotropy
  • Computer Simulation
  • Models, Chemical
  • Nuclear Magnetic Resonance, Biomolecular / methods*
  • Protein Denaturation
  • Proteins / chemistry*

Substances

  • Proteins