Influence of solvent and intramolecular hydrogen bonding on the conformational properties of o-linked glycopeptides.

ABSTRACT: A detailed investigation of the conformational properties of all the biologically relevant O-glycosidic linkages using the Hamiltonian replica exchange (HREX) simulation methodology and the recently developed CHARMM carbohydrate force field parameters is presented. Fourteen biologically relevant O-linkages between the five sugars N-acetylgalactosamine (GalNAc), N-acetylglucosamine (GlcNAc), D-glucose (Glc), D-mannose (Man), and L-fucose (Fuc) and the amino acids serine and threonine were studied. The force field was tested by comparing the simulation results of the model glycopeptides to various NMR (3)J coupling constants, NOE distances, and data from molecular dynamics with time-averaged restraints (tar-MD). The results show the force field to be in overall agreement with experimental an

SUBMITTER: Mallajosyula SS 

PROVIDER: S-EPMC3179525 | biostudies-literature | 2011 Sep

REPOSITORIES: biostudies-literature