Ontology highlight
ABSTRACT:
SUBMITTER: Radford RJ
PROVIDER: S-EPMC2722220 | biostudies-literature | 2009 Jul
REPOSITORIES: biostudies-literature
Journal of the American Chemical Society 20090701 26
We previously devised a strategy (metal-directed protein self-assembly, MDPSA) that utilizes the simultaneous stability, lability, and directionality of metal-ligand bonds to drive protein-protein interactions. Here we show that both the structural and functional scopes of MDPSA can be broadened by incorporation of non-natural metal-chelating ligands onto protein surfaces. A cytochrome cb(562) variant, MBP-Phen1, which features a covalently attached phenanthroline (Phen) group on its surface, se ...[more]