Site-specific backbone dynamics from a crystalline protein by solid-state NMR spectroscopy

J Am Chem Soc. 2004 Sep 22;126(37):11422-3. doi: 10.1021/ja046578g.

Abstract

Site-specific nitrogen-15 longitudinal relaxation rates are measured for the microcrystalline dimeric form of the protein Crh using multidimensional high-resolution solid-state NMR methods. The measured rates are used to provide a qualitative description of the site-specific internal mobility of the protein present in the solid state.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Crystallization
  • Nitrogen Isotopes
  • Nuclear Magnetic Resonance, Biomolecular / methods*
  • Phosphoproteins / chemistry*
  • Protein Conformation
  • Protein Structure, Secondary

Substances

  • Bacterial Proteins
  • Nitrogen Isotopes
  • Phosphoproteins