1 H- 1 H MAS correlation spectroscopy and distance measurements in a deuterated peptide

B. Reif, C. P. Jaroniec, C. M. Rienstra, M. Hohwy, R. G. Griffin

Research output: Contribution to journalEditorial

Abstract

In this Communication, we demonstrate the use of deuteration together with back substitution of exchangeable protons as a means of attenuating the strong 1 H- 1 H couplings that broaden 1 H magic angle spinning (MAS) spectra of solids. The approach facilitates 15 N- 1 H correlation experiments as well as experiments for the measurement of 1 H- 1 H distances. The distance measurement relies on the excellent resolution in the 1 H MAS spectrum and homonuclear double quantum recoupling techniques. The 1 H- 1 H dipolar recoupling can be analyzed in an analytical fashion by fitting the data to a 2- or 3-spin system. The experiments are performed on a sample of the dipeptide N-Ac-Val-Leu-OH, which was synthesized from uniformly [ 2 H, 15 N] labeled materials and back-exchanged in H 2 O.

Original languageEnglish (US)
Pages (from-to)320-327
Number of pages8
JournalJournal of Magnetic Resonance
Volume151
Issue number2
DOIs
StatePublished - Jan 1 2001
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Nuclear and High Energy Physics
  • Condensed Matter Physics

Fingerprint Dive into the research topics of '<sup>1</sup> H- <sup>1</sup> H MAS correlation spectroscopy and distance measurements in a deuterated peptide'. Together they form a unique fingerprint.

  • Cite this