Effect of glycosylation on protein folding: a close look at thermodynamic stabilization.

ABSTRACT: Glycosylation is one of the most common posttranslational modifications to occur in protein biosynthesis, yet its effect on the thermodynamics and kinetics of proteins is poorly understood. A minimalist model based on the native protein topology, in which each amino acid and sugar ring was represented by a single bead, was used to study the effect of glycosylation on protein folding. We studied in silico the folding of 63 engineered SH3 domain variants that had been glycosylated with different numbers of conjugated polysaccharide chains at different sites on the protein's surface. Thermal stabilization of the protein by the polysaccharide chains was observed in proportion to the number of attached chains. Consistent with recent experimental data, the degree of thermal stabilization depende

SUBMITTER: Shental-Bechor D 

PROVIDER: S-EPMC2448824 | biostudies-literature | 2008 Jun

REPOSITORIES: biostudies-literature