Rachel B. Kapust

TL;DR: Maltose‐binding protein seems to be capable of functioning as a general molecular chaperone in the context of a fusion protein, and a model is proposed to explain how MBP promotes the solubility and influences the folding of its fusion partners.

TL;DR: Results suggest that autoinactivation of TEV protease may be an intramolecular reaction that is facilitated by an allosteric interaction between protease molecules.

TL;DR: It is reported that exposure of human cells to NO generated from an NO donor or from overexpression of inducible nitric oxide synthase (NOS2) results in p53 protein accumulation, which provides a novel mechanism by which p53 safeguards against DNA damage through p53-mediated transrepression of NOS2 gene expression, thus reducing the potential for NO-induced DNA damage.

TL;DR: The results indicate that many side-chains can be accommodated in the P1' position of a TEV protease recognition site with little impact on the efficiency of processing.

TL;DR: Analysis of the protein-ligand interactions helps to delineate the structural determinants of substrate specificity and provides guidance for reengineering the enzyme to further improve its utility for biotechnological applications.