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Bengt Nölting

    Protein folding kinetics
    Methods in modern biophysics
    • 2003

      Methods in modern biophysics

      • 254 Seiten
      • 9 Lesestunden
      5,0(2)Abgeben

      Incorporating dramatic recent advances, „Methods in Modern Biophysics“ presents a fresh and timely introduction to modern biophysical methods. This innovative text surveys and explains the ten key biophysical methods, including those related to biophysical nanotechnology, scanning probe microscopy, X-ray crystallography, ion mobility spectrometry, mass spectrometry, and proteomics. Containing much information previously unavailable in tutorial form, „Methods in Modern Biophysics“ employs worked examples and more than 260 illustrations to fully detail the techniques and their underlying mechanisms. The book was written for advanced undergraduate and graduate students, postdocs, researchers, lecturers and professors in biophysics, biochemistry, general biology and related fields.

      Methods in modern biophysics
    • 1999

      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.

      Protein folding kinetics