Enzyme dynamics intramolecular

Effect of enzyme dynamics on catalytic activity, 41, 317 Effective charge and transition-state structure in solution, 27, 1 Effective molarities of intramolecular reactions, 17, 183 Electrical conduction in organic solids, 16, 159 Electrochemical methods, study of reactive intermediates by, 19, 131 Electrochemical recognition of charged and neutral guest species by redox-active receptor molecules, 31, 1... 

In recent years, increasing attention has been focused on proteins derived from extreme thermophylic bacteria (Daniel and Cowan, 2000 Vetriani et al., 1998 Jaenicke, 1996 1998, 2000 Adams and Kelly, 2001 and references therein). The increasing use of these proteins in biotechnology has given new impetus to studies focused on their structure and stability. At the same time, thermostable proteins prove challenging as the ideal candidates for investigating the relationships between the structure and intramolecular dynamics of the enzyme on the one hand, and their function and stability on the other. 

P-glycosidase from the hyperthermophylic archaeon Sulfolobus solfataricus and its recombinants appear to be convenient objects for studying the relationship between intramolecular dynamics and enzyme activity (Nucci et al., 1993 Moracci et al., 1996 D Auria et al., 1998, 1999 Bismuto et al., 1999). The enzyme is barely active up to... 

A minimum requirement for a true enzyme mimic is a binding interaction between two molecules preliminary to the catalytic reaction, indicated by Michaelis-Menten kinetics. Intramolecular systems can support very rapid reactions because we can use synthesis to bring groups together into close and unavoidable proximity. But an enzyme must select and bind its substrate non-covalently in a dynamic equilibrium. The chemistry of... 

For DHFR in particular, molecular dynamics calculations, NMR measurements of solution stracture, and kinetics measurements of mutant forms of the enzyme appear to support the importance of dynamic motions of the protein fold to trigger the reaction of an enzyme-substrate NAC. The mutations in question (for example Glyl20 in Fig. 7) are well removed from the active site and underscore the role of the entire protein fold. The contribution of dynamic motions to the overall catalytic rate remains to be elucidated for the majority of enzymes. Their existence may explain why more rigid molecules such as imprinted polymers and catalytic antibodies do not generally exhibit the large rate accelerations noted with enzymes despite the fact that they too have converted an intermolecular process to an intramolecular process. 

Protein Intramolecular Dynamics and Catalytic Activity of Enzymes. 

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