Image: A lab in the department of biochemistry and molecular biology recently had an article published in the journal Nature. Dr. Zachary Wood's lab published "The entropic force generated by intrinsically disordered segments tunes protein function" on Monday, which shows that disordered peptide segments can shape the energy landscape of proteins in order to optimize a specific function. Proteins are dynamic structures, and are best thought of as an ensemble of interchanging shapes. Keul, et al shows that the entropic force produced by the disordered carboxy terminus of the enzyme human UDP-α-D-glucose-6-dehydrogenase (UGDH) can shift the "conformational ensemble ... towards a substate with a high affinity for an allosteric inhibitor." This finding suggests a reason for the observation that "44% of the human proteome contains intrinsically disordered peptide segments greater than 30 residues in length, the majority of which have no known function." Keul, et al propose that the persistence of intrinsic disorder in the proteome may reflect evolution selecting for disordered segments to tune the energy landscape of proteins. The article is available in full here.
