Solution-phase chemical shift anisotropy as a promising tool to probe intermolecular interactions and peptide bond geometry: A case study on 15N-labeled Nα-t-Boc-L-valine

Katalin E. Kövér, Gyula Batta, Victor J. Hruby

Research output: Contribution to journalArticle

3 Scopus citations

Abstract

Geometry-dependent chemical shift anisotropy (CSAg) values of 1H and 15N nuclei have been determined in solution for 15N-labeled, Nα-t-Boc-L-valine by measurements of CSA/dipole-dipole cross-correlated relaxation rates using longitudinal variants of the recently proposed one-dimensional cross-correlation experiments. We demonstrate that solvent dependence of the CSAg is an invaluable tool for monitoring intermolecular H-bonding interactions. In addition, enhanced temperature dependence was observed for CSAg, which indicates that the anisotropy of chemical shift is more sensitive to subtle changes in the electronic environment of the nucleus than the motionally averaged isotropic chemical shift. 15N CSAg values have been determined in cyclosporin A at natural isotope abundance using the proposed 1H-detected pulse schemes. A remarkable correlation was observed between the measured 15N CSAg and the peptide ω angle, taken from the X-ray structure of cyclosporin A.

Original languageEnglish (US)
Pages (from-to)828-836
Number of pages9
JournalMagnetic Resonance in Chemistry
Volume41
Issue number10
DOIs
StatePublished - Oct 2003

Keywords

  • H and N CSA
  • H, N NMR
  • Intermolecular H-bond
  • Longitudinal CSA/DD cross-correlation
  • NMR
  • Relaxation
  • Relaxation interference
  • Solvent dependence
  • Temperature dependence

ASJC Scopus subject areas

  • Chemistry(all)
  • Materials Science(all)

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