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The similarity of the two correlation functions indicates that dynamical effects do not contribute substantially to catalysis.
How important are quantum mechanical nuclear motions in enzyme catalysis?
Energetically, catalysis is entirely entropic, indicating an important role of solvent reorganization, substrate positioning, and/or orientation of the reacting groups within the active site.
Energetically, catalysis is entirely entropic, indicating an important role of substrate positioning, orientation of the reacting groups within the active site, and solvent reorganization.
These findings suggest that general acid-base catalysis by ribosomal residues does not play a significant role in peptidyl transfer on the ribosome.
As expected, catalysis from the leading edge leads to a significant decrease in the atomic oxygen mass fraction near the surface.
The calculated effects on catalysis, though possibly significant for fine-tuning the kinetics, are relatively small considering the overall catalytic power of these highly efficient enzymes.
What are the roles of substrate-assisted catalysis and proximity effects in peptide bond formation by the ribosome?
Until recently, there has been little direct experimental information on entropic contributions to enzyme catalysis.
It is the apposition of these elements and interaction of imperfections that give rise to diverse molecular interactions and chemical catalysis.
The kinase domain is in equilibrium between an 'open, accessible ' state, subject to phosphorylation, and a 'closed, competent' state, able to perform catalysis.
The result is a small decrease in the thermal heat flux due to the catalysis.
This was his model of physiological combustion, but ignoring the possibility of catalysis.
The catalysis has no significant effect on the shear stress.
Although several simulation studies have suggested that dynamical effects could be important in enzyme catalysis, the evidence, in our view, is not very compelling.
