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

K. Kövér, G. Batta, Victor J. Hruby

Research output: Contribution to journalArticle

3 Citations (Scopus)

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
Pages (from-to)828-836
Number of pages9
JournalMagnetic Resonance in Chemistry
Volume41
Issue number10
Publication statusPublished - Oct 2003

Fingerprint

Valine
Chemical shift
Peptides
peptides
chemical equilibrium
Anisotropy
Cyclosporine
anisotropy
Geometry
probes
geometry
dipoles
nuclei
cross relaxation
interactions
Isotopes
cross correlation
isotopes
X rays
temperature dependence

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)
  • Physical and Theoretical Chemistry
  • Spectroscopy

Cite this

@article{0c4a9b59dd4f4df3b20c1d0c60adc6cc,
title = "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",
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.",
keywords = "H and N CSA, H, N NMR, Intermolecular H-bond, Longitudinal CSA/DD cross-correlation, NMR, Relaxation, Relaxation interference, Solvent dependence, Temperature dependence",
author = "K. K{\"o}v{\'e}r and G. Batta and Hruby, {Victor J.}",
year = "2003",
month = "10",
language = "English",
volume = "41",
pages = "828--836",
journal = "Magnetic Resonance in Chemistry",
issn = "0749-1581",
publisher = "John Wiley and Sons Ltd",
number = "10",

}

TY - JOUR

T1 - Solution-phase chemical shift anisotropy as a promising tool to probe intermolecular interactions and peptide bond geometry

T2 - A case study on 15N-labeled Nα-t-Boc-L-valine

AU - Kövér, K.

AU - Batta, G.

AU - Hruby, Victor J.

PY - 2003/10

Y1 - 2003/10

N2 - 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.

AB - 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.

KW - H and N CSA

KW - H, N NMR

KW - Intermolecular H-bond

KW - Longitudinal CSA/DD cross-correlation

KW - NMR

KW - Relaxation

KW - Relaxation interference

KW - Solvent dependence

KW - Temperature dependence

UR - http://www.scopus.com/inward/record.url?scp=0242267437&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0242267437&partnerID=8YFLogxK

M3 - Article

VL - 41

SP - 828

EP - 836

JO - Magnetic Resonance in Chemistry

JF - Magnetic Resonance in Chemistry

SN - 0749-1581

IS - 10

ER -