Structural analysis of protein interfaces from 13C direct-detected paramagnetic relaxation enhancements

J Am Chem Soc. 2010 Jun 2;132(21):7285-7. doi: 10.1021/ja1014508.

Abstract

The measurement of (13)C directed-detected paramagnetic relaxation enhancements (PREs) on spin-labeled proteins combines the efficacy of PREs for the detection of long-range distance information with the favorable sensitivity and resolution of (13)C direct-detected experiments. The (13)C PREs provide long-range distance restraints to map binding interfaces in proteins and protein complexes and are especially useful for studies of high-molecular weight perdeuterated molecules.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carbon Isotopes / chemistry
  • Electron Spin Resonance Spectroscopy / methods*
  • Nuclear Proteins
  • Protein Conformation
  • Proteins / chemistry*
  • Ribonucleoproteins
  • Spin Labels
  • Splicing Factor U2AF

Substances

  • Carbon Isotopes
  • Nuclear Proteins
  • Proteins
  • Ribonucleoproteins
  • Spin Labels
  • Splicing Factor U2AF