Designability of Aromatic Interaction Networks at E. coli Bacterioferritin B-Type Channels.

ABSTRACT: The bacterioferritin from E. coli (BFR), a maxi-ferritin made of 24 subunits, has been utilized as a model to study the fundamentals of protein folding and self-assembly. Through structural and computational analyses, two amino acid residues at the B-site interface of BFR were chosen to investigate the role they play in the self-assembly of nano-cage formation, and the possibility of building aromatic interaction networks at B-type protein-protein interfaces. Three mutants were designed, expressed, purified, and characterized using transmission electron microscopy, size exclusion chromatography, native gel electrophoresis, and temperature-dependent circular dichroism spectroscopy. All of the mutants fold into α-helical structures and possess lowered thermostability. The double mutan

SUBMITTER: Zhang Y 

PROVIDER: S-EPMC6149950 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature