Protein folding kinetics

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This new method reveals fast processes typically obscured in kinetic studies, offering a broader applicability than presented. It serves as a valuable introduction for those in fast chemical reactions and physical changes, including conformational isomerizations and enzyme kinetics. The framework emphasizes that quantifying kinetic rate constants and visualizing protein structures along the folding pathway enhances understanding of function, mechanism, and significant biological processes and disease states through detailed mechanistic insights. Numerous figures provide unique information, complemented by extensive references to original research papers, reviews, and monographs. Acknowledgments include support from a European Union Human Capital and Mobility Fellowship and a Medical Research Council Fellowship during work at Cambridge University and the Medical Research Council. Special thanks to Prof. Dr. Alan R. Fersht for interest in fast folding reactions, and to Dr. Jose L. Neira and Dr. Andres S. Soler Gonzalez for NMR measurements on barstar peptides. Additionally, work at the University of Illinois at Urbana-Champaign received support from NIH grant GM31756, with particular acknowledgment to Prof. Dr. Steven G. Sligar for his support of acoustic relaxation experiments and insightful discussions.