Impact of sialic acids on the molecular dynamic of bi-antennary and tri-antennary glycans.

ABSTRACT: Sialic acids (SA) are monosaccharides that can be located at the terminal position of glycan chains on a wide range of proteins. The post-translational modifications, such as N-glycan chains, are fundamental to protein functions. Indeed, the hydrolysis of SA by specific enzymes such as neuraminidases can lead to drastic modifications of protein behavior. However, the relationship between desialylation of N-glycan chains and possible alterations of receptor function remains unexplored. Thus, the aim of the present study is to establish the impact of SA removal from N-glycan chains on their conformational behavior. We therefore undertook an in silico investigation using molecular dynamics to predict the structure of an isolated glycan chain. We performed, for the first time, 3 independent 50

SUBMITTER: Guillot A 

PROVIDER: S-EPMC5069492 | biostudies-literature | 2016 Oct

REPOSITORIES: biostudies-literature