Issue 43, 2013

Fast-pulsing NMR techniques for the detection of weak interactions: successful natural abundance probe of hydrogen bonds in peptides

Abstract

Structural investigations of peptides using NMR spectroscopy rarely include the detection of N–H⋯O[double bond, length as m-dash]C and N–H⋯N hydrogen bonds, because the relevant heteronuclei have a low natural abundance while the small trans hydrogen bond scalar couplings reduce the sensitivity. Fast repetition NMR techniques combined with state of the art spectrometer specifications allowed the enhancement of the sensitivity for detection of hydrogen bonds at natural isotopic abundance.

Graphical abstract: Fast-pulsing NMR techniques for the detection of weak interactions: successful natural abundance probe of hydrogen bonds in peptides

Supplementary files

Article information

Article type
Paper
Submitted
13 Sep 2013
Accepted
19 Sep 2013
First published
08 Oct 2013

Org. Biomol. Chem., 2013,11, 7611-7615

Fast-pulsing NMR techniques for the detection of weak interactions: successful natural abundance probe of hydrogen bonds in peptides

A. Altmayer-Henzien, V. Declerck, D. J. Aitken, E. Lescop, D. Merlet and J. Farjon, Org. Biomol. Chem., 2013, 11, 7611 DOI: 10.1039/C3OB41876F

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements