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Conformational Analysis of a High‐Mannose‐Type Oligosaccharide Displaying Glucosyl Determinant Recognised by Molecular Chaperones Using NMR‐Validated Molecular Dynamics Simulation
Author(s) -
Suzuki Tatsuya,
Kajino Megumi,
Yanaka Saeko,
Zhu Tong,
Yagi Hirokazu,
Satoh Tadashi,
Yamaguchi Takumi,
Kato Koichi
Publication year - 2017
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201600595
Subject(s) - molecular dynamics , chemistry , nuclear magnetic resonance spectroscopy , glycosidic bond , oligosaccharide , conformational ensembles , mannose , molecular model , chaperone (clinical) , stereochemistry , biochemistry , computational chemistry , enzyme , medicine , pathology
Exploration of the conformational spaces of flexible oligosaccharides is essential to gain deeper insights into their functional mechanisms. Here we characterised dynamic conformation of a high‐mannose‐type dodecasaccharide with a terminal glucose residue, a critical determinant recognised by molecular chaperones. The dodecasaccharide was prepared by our developed chemoenzymatic technique, which uses 13 C labelling and lanthanide tagging to detect conformation‐dependent paramagnetic effects by NMR spectroscopy. The NMR‐validated molecular dynamics simulation produced the dynamic conformational ensemble of the dodecasaccharide. This determined its spatial distribution as well as the glycosidic linkage conformation of the terminal glucose determinant. Moreover, comparison of our results with previously reported crystallographic data indicates that the chaperone binding to its target oligosaccharides involves an induced‐fit mechanism.