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Hydrogen bonding geometry of a protein-bound carbohydrate from water exchange-mediated cross-relaxation.
- Source :
-
Journal of biomolecular NMR [J Biomol NMR] 1998 Aug; Vol. 12 (2), pp. 209-22. - Publication Year :
- 1998
-
Abstract
- We present heteronuclear two-dimensional methods for the analysis of the geometry of exchangeable protons on a protein-bound carbohydrate. By using a water-selective NOESY-HSQC, we observed cross-relaxation between carbohydrate hydroxyl protons and non-exchangeable ring protons in the complex of [13C6]-alpha-methyl-D-mannopyranoside with recombinant rat mannose binding protein. Using a simple kinetic model, we were able to explain the differences in the initial slopes of the resulting cross-relaxation buildup curves in terms of the geometry of the hydroxyl protons in the bound state. The hydroxyl rotamers consistent with our cross-relaxation data fit very well with predictions based on the crystal structure of MBP bound to a mannose-rich oligosaccharide. These methods should be applicable to other systems where both ligand exchange and water exchange are fast relative to the rate of cross-relaxation.
- Subjects :
- Animals
Carbohydrate Metabolism
Carrier Proteins chemistry
Carrier Proteins genetics
Carrier Proteins metabolism
Escherichia coli genetics
Hydrogen Bonding
In Vitro Techniques
Kinetics
Ligands
Magnetic Resonance Spectroscopy
Mannose-Binding Lectins
Methylmannosides chemistry
Methylmannosides metabolism
Models, Chemical
Oligosaccharides chemistry
Oligosaccharides metabolism
Protein Binding
Proteins metabolism
Rats
Recombinant Proteins chemistry
Recombinant Proteins genetics
Recombinant Proteins metabolism
Water chemistry
Water metabolism
Carbohydrates chemistry
Proteins chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0925-2738
- Volume :
- 12
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Journal of biomolecular NMR
- Publication Type :
- Academic Journal
- Accession number :
- 9751995
- Full Text :
- https://doi.org/10.1023/a:1008220522409