Site-specific ¹⁹F NMR chemical shift and side chain relaxation analysis of a membrane protein labeled with an unnatural amino acid

Protein Sci. 2011 Jan;20(1):224-8. doi: 10.1002/pro.545.

Abstract

Site-specific ¹⁹F chemical shift and side chain relaxation analysis can be applied on large size proteins. Here, one-dimensional ¹⁹F spectra and T₁, T₂ relaxation data were acquired on a SH3 domain in aqueous buffer containing 60% glycerol, and a nine-transmembrane helices membrane protein diacyl-glycerol kinase (DAGK) in dodecyl phosphochoine (DPC) micelles. The high quality of the data indicates that this method can be applied to site-specifically analyze side chain internal mobility of membrane proteins or large size proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Signal Transducing / chemistry*
  • Diacylglycerol Kinase / chemistry*
  • Humans
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Muscle Proteins
  • Phenylalanine / analogs & derivatives
  • Phenylalanine / chemistry
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • src Homology Domains

Substances

  • 4-(trifluoromethyl)phenylalanine
  • Adaptor Proteins, Signal Transducing
  • Muscle Proteins
  • SORBS3 protein, human
  • Phenylalanine
  • Diacylglycerol Kinase