Identification and Characterization of an Inside-Out Folding Intermediate of T4 Phage Sliding Clamp.

ABSTRACT: Protein folding process involves formation of transiently occurring intermediates that are difficult to isolate and characterize. It is both necessary and interesting to characterize the structural conformations adopted by these intermediates, also called molten globules (MG), to understand protein folding. Here, we investigated the equilibrium (un)folding intermediate state of T4 phage gene product 45 (gp45, also known as DNA polymerase processivity factor or sliding clamp) obtained during chemical denaturation. We show that gp45 undergoes substantial conformational rearrangement during unfolding and forms an expanded dry-MG. By monitoring the fluorescence of tryptophans that were strategically introduced at various sites, we demonstrate that the urea-treated molecule has its surface resi

SUBMITTER: Singh MI 

PROVIDER: S-EPMC5647592 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature