Direct observation of carbohydrate hydroxyl protons in hydrogen bonds with a protein

Abstract

Hydroxyl proton resonances of uniformly C-13-labeled Man alpha(1-2)Man alpha(1-2)Man alpha OMe (Man(3)) bound to cyanovirin-N (CV-N) were detected at ambient temperature in aqueous solution by NMR spectroscopy. The directions of the hydroxyl groups were determined on the basis of NOEs, and a previously unknown hydrogen-bonding network between Man(3) and CV-N was discovered. This is the first report on detecting hydroxyl protons of a protein-bound carbohydrate in aqueous solution by NMR. Approaches such as those presented here may open the door for accurately determining intermolecular hydrogen bonds in carbohydrate-protein complexes.

Published in

Journal of the American Chemical Society
2018, volume: 140, number: 1, pages: 339-345
Publisher: AMER CHEMICAL SOC

SLU Authors

• Nestor, Gustav

  • University of Pittsburgh

UKÄ Subject classification

Structural Biology

Publication identifier

• DOI: https://doi.org/10.1021/jacs.7b10595

Permanent link to this page (URI)

https://res.slu.se/id/publ/102271