(15)N-(15)N proton assisted recoupling in magic angle spinning NMR

J Am Chem Soc. 2009 Apr 29;131(16):5769-76. doi: 10.1021/ja806578y.

Abstract

We describe a new magic angle spinning (MAS) NMR experiment for obtaining (15)N-(15)N correlation spectra. The approach yields direct information about the secondary and tertiary structure of proteins, including identification of alpha-helical stretches and interstrand connectivity in antiparallel beta-sheets, which are of major interest for structural studies of membrane proteins and amyloid fibrils. The method, (15)N-(15)N proton assisted recoupling (PAR), relies on a second-order mechanism, third spin assisted recoupling (TSAR), used previously in the context of (15)N-(13)C and (13)C-(13)C polarization transfer schemes. In comparison to (15)N-(15)N proton-driven spin diffusion experiments, the PAR technique accelerates polarization transfer between (15)N's by a factor of approximately 10(2)-10(3) and is furthermore applicable over the entire range of currently available MAS frequencies (10-70 kHz).

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Computer Simulation
  • Escherichia coli / genetics
  • Humans
  • Models, Molecular
  • Mutant Proteins / chemistry
  • Mutant Proteins / genetics
  • Mutant Proteins / isolation & purification
  • Nerve Tissue Proteins / chemistry*
  • Nerve Tissue Proteins / genetics
  • Nerve Tissue Proteins / isolation & purification
  • Nitrogen Isotopes / analysis
  • Nuclear Magnetic Resonance, Biomolecular / methods*
  • Peptides / chemistry*
  • Protein Conformation
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Protons*

Substances

  • G-substrate
  • Mutant Proteins
  • Nerve Tissue Proteins
  • Nitrogen Isotopes
  • Peptides
  • Protons