Companion Blog on Enzyme Function

Today I created a companion blog to this one, dealing with the emerging non-structural evidence in support of the role of constraint in enzyme catalysis. The blog is called "Enzyme Function" and can be viewed by clicking here. The evidence is from measurements of the kinetic isotope effects in enzymic hydride transfer reactions and subsequent attempts to simulate those effects by quantum mechanics. It is found that the effects can be simulated if atoms are brought significantly closer together than their van der Waals radii would allow. In other words the observed kinetic isotope effects imply that the active site is compressed at the time of catalysis. It is the need for compression at the time of catalysis that created the need to look for rigid protein structures as described in the current blog.

Citations of the Biophysics paper that started this blog

So far there are three laboratories that cite this work. Most active is the group of Atsushi Imai in Tokyo. They cite this work as a reason for research into the mechanical properties of single protein molecules. Their citing papers have been published in 2009, 2008, 2007, 2005a, 2005b, 2004a, and 2004b.
Another group is the Yeates group at UCLA. Their 2006 paper on knots in protein folds cited my work as justifying interest in sites of protein rigidity.
A third group (Tsekova and Sakov in Sofia, Bulgaria) published work on protein adsorption in 2005 and cited my work as justifying the study of protein-protein interactions.