B
Brandon Pybus
Researcher at Brandeis University
Publications - 3
Citations - 264
Brandon Pybus is an academic researcher from Brandeis University. The author has contributed to research in topics: Active site & Hydrogen bond. The author has an hindex of 3, co-authored 3 publications receiving 251 citations. Previous affiliations of Brandon Pybus include Stanford University.
Papers
More filters
Journal ArticleDOI
Testing electrostatic complementarity in enzyme catalysis: hydrogen bonding in the ketosteroid isomerase oxyanion hole.
Daniel A. Kraut,Paul A. Sigala,Brandon Pybus,Corey W. Liu,Dagmar Ringe,Gregory A. Petsko,Daniel Herschlag +6 more
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.
Journal ArticleDOI
Testing Geometrical Discrimination within an Enzyme Active Site: Constrained Hydrogen Bonding in the Ketosteroid Isomerase Oxyanion Hole
Paul A. Sigala,Daniel A. Kraut,Jose M. M. Caaveiro,Brandon Pybus,Eliza A. Ruben,Dagmar Ringe,Gregory A. Petsko,Daniel Herschlag +7 more
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.
Journal ArticleDOI
Quantitative dissection of hydrogen bond-mediated proton transfer in the ketosteroid isomerase active site
Paul A. Sigala,Aaron T. Fafarman,Jason P. Schwans,Stephen D. Fried,Timothy D. Fenn,Jose M. M. Caaveiro,Brandon Pybus,Dagmar Ringe,Gregory A. Petsko,Steven G. Boxer,Daniel Herschlag +10 more
TL;DR: This study incorporated spectroscopic probes into the active site of the bacterial enzyme ketosteroid isomerase to systematically dissect the proton transfer equilibrium within a key hydrogen bond network formed to bound transition state analogs, and quantified the electrostatic field changes within the surrounding active site that accompany these rearrangements within the network.