Improved resolution in three-dimensional constant-time triple resonance NMR spectroscopy of proteins

J Biomol NMR. 1992 Jan;2(1):103-8. doi: 10.1007/BF02192804.

Abstract

Two new protocols for the three-dimensional, triple resonance, constant-time HCA(CO)N NMR experiment are presented that significantly increase the experimental resolution attainable in the C alpha frequency dimension. Experimental verification of the new experiments is provided by spectra of the IIA domain of glucose permease from Bacillus subtilis.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Bacillus subtilis / enzymology
  • Magnetic Resonance Spectroscopy / methods*
  • Mathematics
  • Phosphoenolpyruvate Sugar Phosphotransferase System / chemistry*
  • Protein Conformation*
  • Proteins / chemistry*
  • Time Factors

Substances

  • Proteins
  • Phosphoenolpyruvate Sugar Phosphotransferase System
  • phosphoenolpyruvate-glucose phosphotransferase