Covalently modified carboxyl side chains on cell surface leads to a novel method toward topology analysis of transmembrane proteins.

ABSTRACT: The research on transmembrane proteins (TMPs) is quite widespread due to their biological importance. Unfortunately, only a little amount of structural data is available of TMPs. Since technical difficulties arise during their high-resolution structure determination, bioinformatics and other experimental approaches are widely used to characterize their low-resolution structure, namely topology. Experimental and computational methods alone are still limited to determine TMP topology, but their combination becomes significant for the production of reliable structural data. By applying amino acid specific membrane-impermeable labelling agents, it is possible to identify the accessible surface of TMPs. Depending on the residue-specific modifications, new extracellular topology data is gathered

SUBMITTER: Muller A 

PROVIDER: S-EPMC6823493 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature