Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 129, Issue 30, Pages 9458-9467Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja072181b
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Different behavior has been observed for the psi torsion angle of the glycosidic linkages of d-GalNAc-Ser and d-GalNAc-Thr motifs, allowing the carbohydrate moiety to adopt a completely different orientation. In addition, the fact that the water pockets found in alpha-d-GalNAc-Thr differ from those obtained for its serine analogue could be related to the different capability that the two model glycopeptides have to structure the surrounding water. This fact could have important biological inferences (i.e., antifreeze activity).
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