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Review: use of residual dipolar couplings to determine the structure of carbohydrates
Author(s) -
Canales A.,
JiménezBarbero J.,
MartínPastor M.
Publication year - 2012
Publication title -
magnetic resonance in chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0749-1581
DOI - 10.1002/mrc.3888
Subject(s) - chemistry , glycosidic bond , residual dipolar coupling , residual , dipole , nuclear magnetic resonance spectroscopy , flexibility (engineering) , magnetic dipole–dipole interaction , complement (music) , computational chemistry , chemical physics , stereochemistry , organic chemistry , biochemistry , algorithm , statistics , mathematics , complementation , computer science , phenotype , gene , enzyme
Solution nuclear magnetic resonance spectroscopy is especially useful in the carbohydrate field. The measurement of residual dipolar couplings provides long‐range structural information, a valuable complement for the structural study of carbohydrates either in its free form or in the bound state to proteins. They permit to deduce the geometry and the flexibility of the glycosidic linkages, which have a major influence on the conformation of carbohydrates and their overall shape. This article reviews the current application of the residual dipolar couplings methodology to carbohydrates. Copyright © 2012 John Wiley & Sons, Ltd.