Electrostatic Studies Of Carbohydrate Active Enzymes

Most charged or titratable residues reside on the protein surface. Each of such residues will exhibit a titration behaviour that is dependent on the local context around the residue. As a consequence both pH, salt and docking of a ligand into the binding cavity of a protein can be expected to alter the protein electrostatics. Electrostatic interactions are the most long range interactions known. It is widely believed that protein electrostatics plays a major role in the recognition between a protein and its ligand(s). In the present chapter we cover the basic theory of protein electrostatics and illustrate in two case stories how electratic based effects may provide important clues in the interpretation of pH activity profiles for the acid and Taka amylases, as well as in the prediction of functional consequences of protein engineering on Acetobacter xylinum .