By Christopher M. Cheatum, Amnon Kohen (auth.), Judith Klinman, Sharon Hammes- Schiffer (eds.)
Christopher M. Cheatum and Amnon Kohen, courting of Femtosecond–Picosecond Dynamics to Enzyme-Catalyzed H-Transfer. Cindy Schulenburg and Donald Hilvert, Protein Conformational affliction and Enzyme Catalysis. A. Joshua Wand, Veronica R. Moorman and Kyle W. Harpole, a stunning position for Conformational Entropy in Protein functionality. Travis P. Schrank, James O. Wrabl and Vincent J. Hilser, Conformational Heterogeneity in the LID area Mediates Substrate Binding to Escherichia coli Adenylate Kinase: functionality Follows Fluctuations. Buyong Ma and Ruth Nussinov, dependent Crowding and Its results on Enzyme Catalysis. Michael D. day-by-day, Haibo Yu, George N. Phillips Jr and Qiang Cui, Allosteric Activation Transitions in Enzymes and Biomolecular cars: Insights from Atomistic and Coarse-Grained Simulations. Karunesh Arora and Charles L. Brooks III, a number of Intermediates, diversified Conformations, and Cooperative Conformational alterations Underlie the Catalytic Hydride move response of Dihydrofolate Reductase. Steven D. Schwartz, Protein Dynamics and the Enzymatic response Coordinate.
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Extra info for Dynamics in Enzyme Catalysis
3 and in general seem to indicate that proteins rigidify upon binding of tightbinding ligands, that this and other perturbations can alter dynamics across the protein, even tens of Angstroms away from the perturbation, and that those effects on the femtosecond to picosecond time scale are consistent with those reported for nanosecond to microsecond time scale motions as detected by NMR relaxation studies. Since the physical and molecular character of the fast dynamics is different from that of the slower motions, these findings are neither intuitive nor trivial.
The very local behavior of these dynamics is in contrast to what has been seen with CO in other proteins and reflects one of the impacts of the choice of chromophore on the observed dynamics. 7 Carbonic Anhydrase II Carbonic anhydrases are zinc enzymes that catalyze the interconversion of bicarbonate and carbon dioxide. There are many isozymes of carbonic anhydrase and these are found throughout biology. The most common isozyme in mammals is carbonic anhydrase II (CA II), which has very high sequence homology across species.
3 Target Recognition and Binding . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4 Intrinsically Disordered Enzymes . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5 Inducibly Disordered Enzymes . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 6 Designed Disordered Enzymes . . . . . . . . . . . . . . . . . . . . . . . . .
Dynamics in Enzyme Catalysis by Christopher M. Cheatum, Amnon Kohen (auth.), Judith Klinman, Sharon Hammes- Schiffer (eds.)