This three-part treatment translates the technical language of research monographs on the theory of free energy transfer in biology, making the subject more accessible to those entering the field. Designed for upper-level classes in biochemistry or biophysics, it can also be used for independent study. 36 figures. 1989 edition.

Free Energy Transduction in Biology: The Steady-State Kinetic and Thermodynamic Formalism focuses on the steady-state kinetic and thermodynamic formalism related to free energy transduction. As the word ""formalism"" implies, the discussion concerns general principles and methods and not details of proposed mechanisms in the various special cases. Organized into seven chapters, this book first describes the diagram method, which is the main analytical tool in the study of discrete state, cycling system. The next chapter describes the essential topic of cycles and cycle fluxes. Some chapters discuss the more important bioenergetic principles that emerge from the diagram approach. This book is also concerned with somewhat more specialized aspects of the subject (stochastics and fluctuations) and interacting subsystems and multienzyme complexes, including oxidative phosphorylation.

This book contains a description of how quantitative notions from physics and chemistry may be applied to biological systems, in particular those involved in biological free energy transduction. Researchers in the fields of bioenergetics and biochemistry will find this volume to be an excellent, in-depth review of the subject and an invaluable source of information.

This text covers the field of steady-state kinetics from basic principles to the control of the multi-enzyme systems which constitute metabolic pathways. Emphasis is placed on the interpretation of the kinetic behaviour of enzyme-catalyzed reactions in terms of mechanisms. Algorithms are developed which can be implemented in computer programs for the derivation of equations. The treatment of steady-state enzyme kinetics is extended to allosteric enzymes and subunit interactions in polymeric enzymes. Principles are presented which provide for mathematical analysis of the control of multi-enzyme systems. Problems are included at the end of each chapter and their solutions are found at the end of the book. This book will be a useful text for advanced undergraduates and graduate students taking courses in enzyme chemistry and enzyme kinetics.

Over the past few decades numerous scientists have called for a unification of the fields of embryo development, genetics, and evolution. Each field has glaring holes in its ability to explain the fundamental phenomena of life. In this book, the author shows how the phenomenon of cell differentiation, considered in its temporal and spatial aspects during embryogenesis, provides a starting point for a unified theory of multicellular organisms (plants, fungi and animals), including their evolution and genetics. This unification is based on the recent discovery of differentiation waves by the author and his colleagues, described in the appendices, and illustrated by a flip movie prepared by a medical artist. To help the reader through the many fields covered, a glossary is included.This book will be of great value to the researcher and practicing doctors/scientists alike. The research students will receive an in-depth tutorial on the topics covered. The seasoned researcher will appreciate the applications and the gold mine of other possibilities for novel research topics.

The kinetic mechanisms by which enzymes interact with inhibitors and activators, collectively called modifiers, are scrutinized and ranked taxonomically into autonomous species in a way similar to that used in the biological classification of plants and animals. The systematization of the mechanisms is based on two fundamental characters: the allosteric linkage between substrate and modifier and the factor by which a modifier affects the catalytic constant of the enzyme. Combinations of the physically significant states of these two characters in an ancestor-descendant-like fashion reveal the existence of seventeen modes of interaction that cover the needs of total, partial and fine-tuning modulation of enzyme activity. These interactions comprise five linear and five hyperbolic inhibition mechanisms, five nonessential activation mechanisms and two hybrid species that manifest either hyperbolic inhibition or nonessential activation characteristics depending on substrate concentration. Five essential activation mechanisms, which are taxonomically independent of the mentioned basic species, complete the inventory of enzyme modifiers. Often masked under conventional umbrella terms or treated as anomalous cases, all seventeen basic inhibition and nonessential activation mechanisms are represented in the biochemical and pharmacological literature of this and the past century, either in the form of rapid or slow-onset reversible interactions, or as irreversible modification processes. The full potential of enzyme inhibitors and activators can only be appreciated after elucidating the details of their kinetic mechanisms of action exploring the entire range of physiologically significant reactant concentrations. This book highlights the wide spectrum of allosteric enzyme modification in physiological occurrences as well as in pharmacological and biotechnological applications that embrace simple and multiple enzyme-modifier interactions. The reader is guided in the journey through this still partly uncharted territory with the aid of mechanistically-oriented criteria aimed at showing the logical way towards the identification of a particular mechanism.