Protein folding kinetics

1995, 1997a; NOlting, 1996). This new method allows fast processes that would normally be hidden in kinetic studies to be revealed. Of course, the range of applicability of fast kinetic methods is far wider than that presented. Thus, everybody working in the fields of fast chemical reactions and physical changes, such as conformational isomerizations, enzyme kinetics and enzyme mechanisms, might see the book as a useful introduction. The framework that is provided for the readers is the notion that the quantitation of kinetic rate constants and the visualization of protein structures along the folding pathway will lead to an understanding of function and mechanism and will aid the understanding of important biological processes and disease states through detailed mechanistic knowledge. Numerous figures provide useful information not easily found elsewhere, and the book includes copious references to original research papers, relevant reviews and monographs. My work at Cambridge University and the Medical Research Council was supported by a European Union Human Capital and Mobility Fellowship and a Medical Research Council Fellowship. I gratefully acknowledge Prof. Dr. Alan R. Fersht for the interest in our work on fast folding reactions. NMR measurements on peptides of barstar were done by Dr. Jose L. Neira and Dr. Andres S. Soler Gonzalez. The work at the University of Illinois at Urbana-Champaign was supported by NIH grant GM31756. Prof. Dr. Steven G. Sligar is particularly acknowledged for his support of acoustic relaxation experiments and many fruitful discussions.