Conspectus As is well-known, enzymes are proteins designed to accelerate specific life
essential chemical reactions by many orders of magnitude. A folded protein is a highly …

Homo-oligomeric protein assemblies are known to participate in dynamic association/
disassociation equilibria under native conditions, thus creating an equilibrium of assembly …

The aim of the book is to introduce the reader to the kinetic analysis of a wide range of
biological processes at the molecular level. It is intended to show that the same approach …

The binding of substrates to lactate dehydrogenases induces a marked rearrangement of
the protein structure in which a 'loop'of polypeptide (residues 98–110) closes over the active …

Analysis of the mechanism and structure of lactate dehydrogenases is summarized in a map
of the catalytic pathway. Chemical probes, single tryptophan residues inserted at specific …

Classic techniques for simulating molecular motion, such as the Monte Carlo and molecular
dynamics methods, generate individual motion pathways one at a time and spend most of …

Abstract Lactate dehydrogenase (LDH, EC. 1.1. 127) is an important enzyme engaged in the
anaerobic metabolism of cells, catalyzing the conversion of pyruvate to lactate and NADH to …

Department of Biochemistry, University of Bristol Medical School, University Walk, Bristol
BS8 1TD, UK, and Microbial Technology Laboratory, PHLS Centre for Applied Microbiology …

The kinetics of internal electron transfer in human cytochrome P450 reductase have been
studied using temperature-jump relaxation spectroscopy. Temperature perturbation of CPR …

We examine here the dynamics of forming the Michaelis complex of the enzyme lactate
dehydrogenase by characterizing the binding kinetics and thermodynamics of oxamate (a …