Measurement of cross correlation between dipolar coupling and chemical shift anisotropy in the spin relaxation of 13C, 15N-labeled proteins

J Magn Reson. 1998 Dec;135(2):487-99. doi: 10.1006/jmre.1998.1602.


We present a simple method for extracting interference effects between chemical shift anisotropy (CSA) and dipolar coupling from spin relaxation measurements in macromolecules, and we apply this method to extracting cross-correlation rates involving interference of amide 15N CSA and 15N-1H dipolar coupling and interference of carbonyl 13C' CSA and 15N-13C' dipolar coupling, in a small protein. A theoretical basis for the interpretation of these rates is presented. While it proves difficult to quantitatively separate the structural and dynamic contributions to these cross-correlation rates in the presence of anisotropic overall tumbling and a nonaxially symmetric chemical shift tensor, some useful qualitative correlations of data with protein structure can be seen when simplifying assumptions are made.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Triphosphatases / chemistry
  • Algorithms
  • Bacterial Proteins / chemistry
  • Carbon Isotopes
  • Electron Spin Resonance Spectroscopy
  • Escherichia coli
  • HSP40 Heat-Shock Proteins
  • Heat-Shock Proteins / chemistry
  • Macromolecular Substances
  • Magnetic Resonance Spectroscopy / methods*
  • Models, Chemical
  • Nitrogen Isotopes
  • Protein Conformation
  • Proteins / analysis
  • Proteins / chemistry*
  • Rotation


  • Bacterial Proteins
  • Carbon Isotopes
  • HSP40 Heat-Shock Proteins
  • Heat-Shock Proteins
  • Macromolecular Substances
  • Nitrogen Isotopes
  • Proteins
  • Adenosine Triphosphatases