Perturbing the folding energy landscape of the bacterial immunity protein Im7 by site-specific N-linked glycosylation.

ABSTRACT: N-linked glycosylation modulates protein folding and stability through a variety of mechanisms. As such there is considerable interest in the development of general rules to predict the structural consequences of site-specific glycosylation and to understand how these effects can be exploited in the design and development of modified proteins with advantageous properties. In this study, expressed protein ligation is used to create site-specifically glycosylated variants of the bacterial immunity protein Im7 modified with the chitobiose disaccharide (GlcNAc-GlcNAc). Glycans were introduced at seven solvent exposed sites within the Im7 sequence and the kinetic and thermodynamic consequences of N-linked glycosylation analyzed. The ΔΔG° values for glycan incorporation were found to range from

SUBMITTER: Chen MM 

PROVIDER: S-EPMC3012502 | biostudies-literature | 2010 Dec

REPOSITORIES: biostudies-literature