Review: use of residual dipolar couplings to determine the structure of carbohydrates

被引:17
作者
Canales, A. [1 ]
Jimenez-Barbero, J. [2 ]
Martin-Pastor, M. [3 ]
机构
[1] Univ Complutense Madrid, Dept Organ Chem, Madrid, Spain
[2] CIB CSIC, Madrid 28040, Spain
[3] Univ Santiago de Compostela, Unidade Resonancia Magnet, RIAIDT, La Coruna 15706, Spain
关键词
NMR; H-1; C-13; residual dipolar couplings; carbohydrates; oligosaccharides; flexibility; bound state; HIGH-RESOLUTION NMR; PROTEIN-STRUCTURE; CONFORMATIONAL FLEXIBILITY; BIOLOGICAL MACROMOLECULES; ALIGNMENT; CONSTANTS; DYNAMICS; PROTON; OLIGOSACCHARIDES; BIOMOLECULES;
D O I
10.1002/mrc.3888
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
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 (C) 2012 John Wiley & Sons, Ltd.
引用
收藏
页码:S80 / S85
页数:6
相关论文
共 67 条
[1]   Molecular symmetry as an aid to geometry determination in ligand protein complexes [J].
Al-Hashimi, HM ;
Bolon, PJ ;
Prestegard, JH .
JOURNAL OF MAGNETIC RESONANCE, 2000, 142 (01) :153-158
[2]   Physical interpretation of residual dipolar couplings in neutral aligned media [J].
Almond, A ;
Axelsen, JB .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2002, 124 (34) :9986-9987
[3]   Weakly aligned biological macromolecules in dilute aqueous liquid crystals [J].
Annila, A ;
Permi, P .
CONCEPTS IN MAGNETIC RESONANCE PART A, 2004, 23A (01) :22-37
[4]  
[Anonymous], NMR SPECTROSCOPY GLY
[5]  
Ardá A, 2009, SPR CARB CH, V35, P333, DOI 10.1039/b901565p
[6]   Tracking alignment from the moment of inertia tensor (TRAMITE) of biomolecules in neutral dilute liquid crystal solutions [J].
Azurmendi, HF ;
Bush, CA .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2002, 124 (11) :2426-2427
[7]   Weak alignment offers new NMR opportunities to study protein structure and dynamics [J].
Bax, A .
PROTEIN SCIENCE, 2003, 12 (01) :1-16
[8]  
Blackledge M., 2011, BIOCHEMISTRY-US, V50, P2735
[9]   Validation of protein structure from anisotropic carbonyl chemical shifts in a dilute liquid crystalline phase [J].
Cornilescu, G ;
Marquardt, JL ;
Ottiger, M ;
Bax, A .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1998, 120 (27) :6836-6837
[10]  
de Alba A., 2002, PROG NMR SPECTROSC, V40, P175