Probing carbohydrate-protein interactions by high-resolution NMR spectroscopy

S W Homans, R A Field, M J Milton, M Probert, J M Richardson

Research output: Chapter in Book/Report/Conference proceedingChapter (peer-reviewed)peer-review

Abstract

An important requirement for a detailed understanding of the molecular basis of the interaction of a carbohydrate with its protein receptor is a high-resolution three dimensional structure of the complex. Historically, such structural information has derived from crystallographic studies which can illustrate in detail the precise nature of certain carbohydrate-protein interactions in the solid state (reviewed by Cambillau (1995)). In contrast, few high-resolution structural studies of glycan-protein interactions in solution using nuclear magnetic resonance have been reported. The solution structure of the complex is of importance since a comparison with the solution structure of the free ligand may be more meaningful, and moreover the dynamics of the system are accessible from relaxation time measurements.
Original languageEnglish
Title of host publicationGlycoimmunology 2
Pages29-38
Number of pages10
Volume435
ISBN (Electronic)978-1-4615-5383-0
DOIs
Publication statusPublished - 1998

Publication series

NameAdvances in Experimental Medicine and Biology
PublisherSpringer New York
ISSN (Print)0065-2598

Keywords

  • resonance assignment
  • glycosidic linkage
  • nuclear overhauser effect
  • carbohydrate ligand
  • adjacent monomer

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