By Jo M. Holt, Michael L. Johnson, Gary K. Ackers
This quantity specializes in equipment relating to allosteric enzymes and receptors, together with fluorescent proves, spectroscopic equipment and quantitative research in addition to on cooperativity in protein folding. NMR and mass spectrometry tools are mentioned. *Allosteric Enzymes and Receptors *Cooperativity in Protein Folding and meeting
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20  allosteric enzymes and receptors  Structural Interpretation of pH and Salt-Dependent Processes in Proteins with Computational Methods By Bertrand Garcı´a-Moreno E. and Carolyn A. Fitch Introduction It is widely recognized that electrostatics plays a significant role in modulating the structure, the stability, and the function of proteins. The study of protein electrostatics continues to be of interest because they are of paramount biological importance—most biochemical processes are governed by electrostatics.
Short, and R. Wolfenden, Biochemistry 39, 9746 (2000).  packing improvements within enzymes and receptors 15 ground state to the transition state. The data are consistent with an improvement in bonding within the enzyme during this transformation. The efficiency of enzyme catalysis can be measure in terms of the rate ratio of the enzyme-catalyzed and non-catalyzed reactions (kcat/knon). The enthalpic (bonding) component of this difference has been measured by Wolfenden and co-workers20,21 for reactions catalyzed by six enzymes.
Antosiewicz, and A. D. Robertson, Proteins Struct. Funct. Genet. 48, 388 (2002). 7  electrostatic calculations with proteins 25 Fig. 1. Simulation of the Hþ titration curves of an ionizable residue that titrates with pKa ¼ 3 when the macromolecule is in state A and with pKa ¼ 8 when the macromolecule is in state B. The pH dependence of the free energy difference between states A and B, plotted with reference to the right ordinate, was calculated by integration of the area between the two titration curves with Eq.
Energetics of Biological Macromolecules by Jo M. Holt, Michael L. Johnson, Gary K. Ackers