Intramolecular 1H-13C distance measurement in uniformly 13C, 15N labeled peptides by solid-state NMR

Solid State Nucl Magn Reson. 2012 Jul-Sep:45-46:51-8. doi: 10.1016/j.ssnmr.2012.06.001. Epub 2012 Jun 15.

Abstract

A (1)H-(13)C frequency-selective REDOR (FS-REDOR) experiment is developed for measuring intramolecular (1)H-(13)C distances in uniformly (13)C, (15)N-labeled molecules. Theory and simulations show that the experiment removes the interfering homonuclear (1)H-(1)H, (13)C-(13)C and heteronuclear (1)H-(15)N, (13)C-(15)N dipolar interactions while retaining the desired heteronuclear (1)H-(13)C dipolar interaction. Our results indicate that this technique, combined with the numerical fitting, can be used to measure a (1)H-(13)C distance up to 5Å. We also demonstrate that the measured intramolecular (1)H-(13)C distances are useful to determine dihedral angles in proteins.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Histidine / chemistry
  • Magnetic Resonance Spectroscopy / methods*
  • N-Formylmethionine Leucyl-Phenylalanine / chemistry
  • Peptides / chemistry*

Substances

  • Peptides
  • Histidine
  • N-Formylmethionine Leucyl-Phenylalanine