Ca. Bush et al., Structure and conformation of complex carbohydrates of glycoproteins, glycolipids, and bacterial polysaccharides, ANN R BIO B, 28, 1999, pp. 269
Citations number
150
Categorie Soggetti
Biochemistry & Biophysics
Journal title
ANNUAL REVIEW OF BIOPHYSICS AND BIOMOLECULAR STRUCTURE
For nuclear magnetic resonance determinations of the conformation of oligos
accharides in solution, simple molecular mechanics calculations and nuclear
Overhauser enhancement measurements are adequate for small oligosaccharide
s that adopt single, relatively rigid conformations. Polysaccharides and la
rger or more flexible oligosaccharides generally require additional types o
f data, such as scalar and dipolar coupling constants, which are most conve
niently measured in C-13-enriched samples. Nuclear magnetic resonance relax
ation data provide information on the dynamics of oligosaccharides, which i
nvolves several different types of internal motion. Oligosaccharides comple
xed with lectins and antibodies have been successfully studied both by X-ra
y crystallography and by nuclear magnetic resonance spectroscopy. The compl
exes have been shown to be stabilized by a combination of polar hydrogen bo
nding interactions and van der Waals attractions. Although theoretical calc
ulations of the conformation and stability of free oligosaccharides and of
complexes with proteins can be carried out by molecular mechanics methods,
the role of solvent water for these highly polar molecules continues to pre
sent computational problems.