Daniel A. Kraut

TL;DR: The promise of advancing and integrating cutting edge conceptual, experimental, and computational tools brings mechanistic enzymology to a new era, one poised for novel fundamental insights into biological catalysis.

TL;DR: It is proposed that geometrical complementarity between theOxyanion hole hydrogen-bond donors and the transition state oxyanion provides a significant catalytic contribution, and it is suggested that KSI, like other enzymes, achieves its catalytic prowess through a combination of modest contributions from several mechanisms rather than from a single dominant contribution.

TL;DR: This work aims to provide a systematic literature review and meta-analyses of the determinants of protein Dynamics that have been implicated in infectious disease and Huntington’s disease.

TL;DR: The results strongly suggest that packing and binding interactions within the KSI active site can constrain local side-chain reorientation and prevent hydrogen bond shortening by 0.1 A or less and provide evidence that subtle geometric effects, indistinguishable in most X-ray crystallographic structures, can have significant energetic consequences.

TL;DR: Comparisons of the abilities of representatives from all classes of ATP-dependent proteases to unfold a model substrate protein find that the unfolding abilities range over more than 2 orders of magnitude.