NMR Analysis of Glycosyltransferases

Thomas Peters*

*Corresponding author for this work


Glycosyltransferases are responsible for the biosynthesis of a multitude of complex glycan chains located on cell surfaces, and representing a ″postal code system″ for cell-cell or cell-pathogen recognition. A substantial number of crystal structures of glycosyltransferases have become available showing that these enzymes undergo significant conformational changes upon binding to substrates. Yet, not much is known about the protein dynamics behind these changes. Although NMR offers powerful tools to obtain insight into dynamical processes application to glycosyltransferases has been sparse mainly because of the large size of most of these enzymes rendering especially protein NMR approaches difficult or even impossible. This review highlights studies focussing on the application of NMR experiments to study dynamical aspects of glycosyltransferases. A methodological division is made into protein-based and ligand-based techniques. From the NMR experimental data available it becomes clear that glycosyltransferases are enzymes with a large degree of plasticity.

Original languageEnglish
Title of host publicationBiophysics and Biochemistry of Cartilage by NMR and MRI
EditorsWilliam S. Price, Koichi Kato, Thomas Peters
Number of pages15
PublisherRoyal Society of Chemistry
Publication date17.05.2017
ISBN (Electronic)9781782621331, 9781782623106, 9781849736190
Publication statusPublished - 17.05.2017

Research Areas and Centers

  • Academic Focus: Center for Infection and Inflammation Research (ZIEL)


Dive into the research topics of 'NMR Analysis of Glycosyltransferases'. Together they form a unique fingerprint.

Cite this