Rikkert Wierenga and Rajaram Venkatesan

Rikkert Wierenga Short CV

Rajaram Venkatesan Short CV

Structural Enzymology: A Quantitative Approach

Enzymes have the unique property of converting a bound molecule, the reactant, into another molecule, the product. The (very) high energy barrier between reactant and product somehow (almost) disappears once the reactant is bound in the active site pocket of the enzyme. Understanding of this phenomenon, known as biocatalysis, is one of the main aims of much current enzyme research, pointing to the importance of the electrostatic properties as well as the dynamics of the active site. Protein crystallographic studies provide the three dimensional structure of the active site, how the atoms are arranged, as well as, to some extent, the dynamic properties of the active site residues. Detailed analysis of the structures, including bioinformatics and biocomputing approaches, is an essential component of our structural studies. In addition we complement our structural studies with biophysical characterisation and enzyme kinetic experiments.

Project details

  1. Background and significance
  2. Recent progress
  3. Future goals
  4. Selected publications
  5. Research group members
  6. National and International significance
     

Teaching material (Internal info)

Basic principles of protein crystallography
Structural enzymology


 


 



 

Last updated: 28/10/2016