Title of article :
GROMOS96 43a1 performance in predicting oligosaccharide conformational ensembles within glycoproteins Original Research Article
Author/Authors :
C.L. Fernandes، نويسنده , , L.G. Sachett، نويسنده , , L. Pol-Fachin، نويسنده , , H. Verli، نويسنده ,
Issue Information :
دوهفته نامه با شماره پیاپی سال 2010
Pages :
9
From page :
663
To page :
671
Abstract :
In previous work [Pol-Fachin, L.; Fernandes, C. L.; Verli, H.; Carbohydr. Res. 2009, 344, 491–500], we had demonstrated that GROMOS96 43a1 force field and Löwdin HF/6-31G∗∗-derived atomic charges, adequately represent a glycoprotein’s conformational ensemble in aqueous solutions, taking as the starting geometries NMR-determined structures. Based on such data, the present work intends to evaluate the use of the main solution conformations of isolated disaccharides, to build the carbohydrate moiety of glycoproteins, for which no previous experimental information is available. The observed results suggested that the entire glycoprotein scaffold appears unable to promote major modifications in the conformational behavior of glycosidic linkages. Additionally, when compared to energy contour plots, the results support the use of solution ensembles, to refine vacuum conformations of carbohydrate databases in the assembling of glycoproteins 3D structures. Finally, such approach is applied to build a full glycosylated model for COX-1 and COX-2 enzymes.
Keywords :
Glycosidic linkage , molecular dynamics , GROMOS96 , Carbohydrates , Glycoproteins
Journal title :
Carbohydrate Research
Serial Year :
2010
Journal title :
Carbohydrate Research
Record number :
966924
Link To Document :
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