Protein Folding Kinetics : Biophysical Methods

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. The book imparts insight into the principles and concepts of the kinetic and structural resolution of fast chemical and biophysical reactions of proteins with emphasis on protein folding reactions. The study of fast protein folding reactions and the understanding of the folding paradox have advanced upon the recent development of new biophysical methods which enable not only kinetic resolution in the sub-millisecond time scale but also higher structural resolution. The pathways and structures of early folding events and the transition state structures of fast folding proteins can now be studied in far more detail. Important techniques include biophysical, chemical, molecular biological and mathematical methods, in particular protein engineering, F-value analysis, circular dichroism, fluorescence, pulsed LASER spectroscopy, temperature jumping, ultrafast mixing, and stopped flow. Front Matter....Pages I-XIII Introduction....Pages 1-4 Structures of proteins....Pages 5-15 Physical interactions that determine the properties of proteins....Pages 17-25 Calculation of the kinetic rate constants....Pages 27-49 High kinetic resolution of protein folding events....Pages 51-77 Kinetic methods for slow reactions....Pages 79-82 Resolution of protein structures in solution....Pages 83-93 High structural resolution of transient protein conformations....Pages 95-123 Experimental problems of the kinetic and structural resolution of reactions that involve proteins....Pages 125-136 The folding pathway of a protein (barstar) at the resolution of individual residues from microseconds to seconds....Pages 137-164 Conclusions....Pages 165-166 Back Matter....Pages 167-191 First methods book which includes many detailed descriptions Absolutely needed and thus timely for the scientific community Comprises 15% more content and includes the mentioned special features