The role of action potentials in local calcium signalling and induction of different forms of LTP

Enzymes catalyze quite fantastic chemistry under mild physiological conditions. Uniquely for a catalyst, these powers are integral to the structure, properties and dynamics of the protein, as selected by biological evolution. The challenge is to dissect the contributions the protein makes to catalysis for particular enzymes. Such definition requires energetic and thermodynamic analysis beyond current experimental techniques, but accessible by computer simulation. We aim to study the coupling of changes in protein conformation changes and electrostatics (charge) on a particular enzyme reaction mechanism, as our earlier work suggests these as separately the two major contributions. We suspect that their combined effect will be amplified.