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|a 9783540272786
|9 978-3-540-27278-6
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|a 10.1007/b138868
|2 doi
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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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|a 2nd ed. 2006.
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|a Berlin, Heidelberg :
|b Springer Berlin Heidelberg :
|b Imprint: Springer,
|c 2006.
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|a XVI, 222 p. 170 illus., 12 illus. in color.
|b online resource.
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|a text
|b txt
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|a computer
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|a online resource
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|a text file
|b PDF
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|a Structures of proteins -- Physical interactions that determine the properties of proteins -- Calculation of the kinetic rate constants -- High kinetic resolution of protein folding events -- Kinetic methods for slow reactions -- Resolution of protein structures in solution -- High structural resolution of transient protein conformations -- Experimental problems of the kinetic and structural resolution of reactions that involve proteins -- The folding pathway of a protein (barstar) at the resolution of individual residues from microseconds to seconds -- Highly resolved folding pathways and mechanisms of six proteins -- Structural determinants of the rate of protein folding -- Evolutionary computer programming of protein structure and folding -- Conclusions.
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|a The book gives a deep 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 significantly advanced due to the recent development of new biophysical methods which allow not only kinetic resolution in the sub-millisecond time scale but also structural resolution with unprecedented precision. Pathways and structures of early and late folding events and the transition state structures of fast- and ultrafast-folding proteins can now be studied in far more detail. Important techniques include biophysical, chemical, molecular biological and mathematical methods, in particular protein engineering, Phi-value analysis, time-resolved circular dichroism, optical triggers and pulsed infrared LASER methods, pressure and temperature jump, ultrafast mixing, stopped flow and quenched flow, dielectric relaxation and electric-field-jump, acoustic relaxation, fluorescence- and isotope-labeling, H/D exchange methods, NMR line broadening and stopped-flow NMR, transition state theory, solutions of rate equations, and evolutionary computer programming. Protein Folding Kinetics - Biophysical Methods is written for students and researchers in biochemistry, biophysics, and related fields. Special features in the second edition: • Includes detailed information and 12 color figures on the high resolution of folding transition states. • Discusses structural determinants of the rate of protein folding on a timescale from microseconds to seconds. • Provides information on self-evolving computer programs for protein-folding simulations and protein-structure predictions.
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|a Proteins .
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|a Biochemistry.
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|a Biophysics.
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|a Biotechnology.
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|a Food science.
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|a Protein Biochemistry.
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|a Biochemistry.
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|a Biophysics.
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|a Biotechnology.
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|a Food Science.
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|a SpringerLink (Online service)
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|t Springer Nature eBook
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|i Printed edition:
|z 9783642066047
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|i Printed edition:
|z 9783540812883
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|i Printed edition:
|z 9783540272779
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|u https://doi.uam.elogim.com/10.1007/b138868
|z Texto Completo
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|a ZDB-2-SBL
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|a ZDB-2-SXB
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|a Biomedical and Life Sciences (SpringerNature-11642)
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950 |
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|a Biomedical and Life Sciences (R0) (SpringerNature-43708)
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