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|a 9783662039663
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|a 10.1007/978-3-662-03966-3
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|a Nölting, Bengt.
|e author.
|4 aut
|4 http://id.loc.gov/vocabulary/relators/aut
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|a Protein Folding Kinetics
|h [electronic resource] :
|b Biophysical Methods /
|c by Bengt Nölting.
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| 250 |
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|a 1st ed. 1999.
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| 264 |
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|a Berlin, Heidelberg :
|b Springer Berlin Heidelberg :
|b Imprint: Springer,
|c 1999.
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|a XIII, 191 p. 40 illus.
|b online resource.
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|a Springer eBook Collection
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|a 1 Introduction -- 2 Structures of proteins -- 3 Physical interactions that determine the properties of proteins -- 4 Calculation of the kinetic rate constants -- 5 High kinetic resolution of protein folding events -- 6 Kinetic methods for slow reactions -- 7 Resolution of protein structures in solution -- 8 High structural resolution of transient protein conformations -- 9 Experimental problems of the kinetic and structural resolution of reactions that involve proteins -- 10 The folding pathway of a protein (barstar) at the resolution of individual residues from microseconds to seconds -- 11 Conclusions -- References.
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|a 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.
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|a Loaded electronically.
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|a Electronic access restricted to members of the Holy Cross Community.
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|a Proteins .
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|a Biochemistry.
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|a Biological physics.
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|a Biotechnology.
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|a Food—Biotechnology.
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