The aim of this blog is to encourage development and dissemination of knowledge of native protein structures at the quaternary level, that is, knowledge of the arrangements of subunits in functional proteins. The fundamental starting point of this discussion is that the arrangements seen in protein crystals are not necessarily the native arrangements.
Tuesday, December 28, 2010
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.
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