Energetics-based protein profiling on a proteomic scale: identification of proteins resistant to proteolysis.

ABSTRACT: Native states of proteins are flexible, populating more than just the unique native conformation. The energetics and dynamics resulting from this conformational ensemble are inherently linked to protein function and regulation. Proteolytic susceptibility is one feature determined by this conformational energy landscape. As an attempt to investigate energetics of proteins on a proteomic scale, we challenged the Escherichia coli proteome with extensive proteolysis and determined which proteins, if any, have optimized their energy landscape for resistance to proteolysis. To our surprise, multiple soluble proteins survived the challenge. Maltose binding protein, a survivor from thermolysin digestion, was characterized by in vitro biophysical studies to identify the physical origin of proteolyt

SUBMITTER: Park C 

PROVIDER: S-EPMC2857998 | biostudies-literature | 2007 May

REPOSITORIES: biostudies-literature