Abstract

This chapter discusses relaxation spectrometry of biological systems. The introduction of relaxation techniques as methods for studying chemical kinetics in liquid solutions took place in early times. Since then the use of relaxation methods has produced exciting new results in many different areas of chemistry. This chapter illustrates that the underlying principle of all relaxation techniques is similar—namely, by rapidly changing some external parameter (e.g., temperature or pressure) the thermodynamic state of the system is changed— kinetic studies are made by measurement of the rate of change of concentrations as they approach the new thermodynamic state. Moreover many reactions of biological interest (e.g., enzymatic reactions) are quite rapid; therefore, this feature of relaxation methods is of importance in the study of mechanisms of biological reactions. This chapter discusses the principles and experimental techniques involved in relaxation spectrometry. The chapter also addresses experimental techniques. This chapter concludes by discussing specific studies of the relaxation spectra of biochemical or closely related systems.

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