Although several simulation studies have suggested that dynamical effects could be important in enzyme catalysis, the evidence, in our view, is not very compelling.
The catalysis has no significant effect on the shear stress.
This was his model of physiological combustion, but ignoring the possibility of catalysis.
The result is a small decrease in the thermal heat flux due to the catalysis.
The kinase domain is in equilibrium between an 'open, accessible ' state, subject to phosphorylation, and a 'closed, competent' state, able to perform catalysis.
It is the apposition of these elements and interaction of imperfections that give rise to diverse molecular interactions and chemical catalysis.
Until recently, there has been little direct experimental information on entropic contributions to enzyme catalysis.
What are the roles of substrate-assisted catalysis and proximity effects in peptide bond formation by the ribosome?
