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Full Description
Modern enzymology can no longer rely upon indirect inferences derived by steady state kinetic analysis because these are often misleading. Rather, in the era of "New Enzymology", reactions at the active sites of enzyme are monitored by direct measurement of individual steps in the sequence to establish the pathway of reactions occurring. These quantitative methods can be directly related to high resolution structural information and define the underlying kinetic and thermodynamic basis for catalysis. The goal of a comprehensive kinetic analysis is to identify each step in the reaction pathway, define the rate and equilibrium constants for each step, identify all conformational and chemical intermediates, identify the rate-limiting steps, and ultimately establish the basis for enzymatic specificity and efficiency. This volume contains chapters contributed by leading experts in the application of modern kinetic methods to complex problems in the study of catalysis by both proteins and RNA catalysts.
Contents
1. Introduction to kinetic analysis of enzyme systems ; 2. Detection and characterisation of enzyme intermediates ; 3. Kinetic analysis of DNA-Protein Interactions by time-resolved synchrotron X-ray footprinting ; 4. Kinetic analysis of ribozyme cleavage ; 5. Transient-state kinetics and computational analysis of transcription initiation ; 6. A fluorescent sensor to assay inorganic phosphate ; 7. What to do if there is no signal ; 8. The biotin regulatory system-kinetic, themodynamic and structural interrogation of a biological switch ; 9. Time resolved spectral analysis ; 10. Kinetic analysis of enzyme mutants for identification of catalytic residues
