Encyclopedia of Biophysics

Living Edition
| Editors: Gordon Roberts, Anthony Watts, European Biophysical Societies

Kinetics: Overview

  • Clive R. BagshawEmail author
Living reference work entry

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DOI: https://doi.org/10.1007/978-3-642-35943-9_54-2



The root of Kinetics comes from kinesis (movement), and in general, it is a term applied to characterization of phenomena with respect to time. Every measurement is carried out as a function of time, and hence, there is potentially a kinetic element to every experiment. This section focuses on chemical kinetics which involves the investigation and interpretation of reaction rates. Here the concentrations of chemical species or states are measured with time, principally for the determination of reaction mechanism. Kinetics may also be used empirically to determine the concentrations of species. This is the main-stay of many clinical assays.

Kinetics is fundamental to many aspects of protein and nucleic acid chemistry, be it ligand binding, catalysis, or folding (Bagshaw 2017; Goodrich and Kugel 2006; Gutfreund 1995; Purich 2010). Clearly kinetic studies are central to the characterization of enzymes as catalysts, and many of the principles of...

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  1. Aquila A, Hunter MS, Doak RB et al (2012) Time-Resolved Protein Nanocrystallography Using an X-Ray Free-Electron Laser. Opt Express 20:2706–2716CrossRefPubMedPubMedCentralGoogle Scholar
  2. Bagshaw CR (2017) Biomolecular kinetics: a step-by-step guide. CRC Press, Boca RatonCrossRefGoogle Scholar
  3. Barman TE, Travers F (1985) The rapid-flow-quench method in the study of fast reactions in biochemistry: extension to subzero conditions. Meth Biochem Anal 31:1–59Google Scholar
  4. Bernasconi CF (1976) Relaxation kinetics. Academic, New YorkGoogle Scholar
  5. Chaiken I, Rose S, Karlsson R (1992) Analysis of macromolecular interactions using immobilized `ligands. Anal Biochem 201:197–210CrossRefPubMedGoogle Scholar
  6. Cook PF, Cleland WW (2007) Enzyme kinetics and mechanism. Talyor & Francis, New YorkGoogle Scholar
  7. Cornish-Bowden A (1995) Fundamentals of enzyme kinetics, 2nd edn. Portland Press, LondonGoogle Scholar
  8. de Mol NJ (2010) Fischer MJE surface Plasmon resonance: methods and protocols. Methods Mol Biol 627:255Google Scholar
  9. Eccleston JF, Hutchinson JP, White HD (2001) Stopped-flow techniques. In: Harding SE, Chowdhry BZ (eds) Protein-ligand interactions. Oxford. Oxford University Press, New York, pp 201–237Google Scholar
  10. Engel PC (1981) Enzyme kinetics: the steady-state approach. Chapman and Hall, LondonCrossRefGoogle Scholar
  11. Gell C, Brockwell D, Smith A (2006) Handbook of single molecule fluorescence spectroscopy. Oxford University Press, OxfordGoogle Scholar
  12. Goodrich JA, Kugel JF (2006) Binding and kinetics for molecular biologists. Cold Spring Harbor Laboratory Press, New YorkGoogle Scholar
  13. Goody RS (2014) How not to do kinetics: examples involving GTPases and guanine nucleotide exchange factors. FEBS J 281:593–600CrossRefPubMedGoogle Scholar
  14. Gutfreund H (1995) Kinetics for the life sciences: receptors transmitters and catalysts. Cambridge University Press, CambridgeCrossRefGoogle Scholar
  15. Hiromi K (1979) Kinetics of fast enzyme reactions: theory and practice. Wiley, New YorkGoogle Scholar
  16. Johnson KA (ed) (2003) Kinetic analysis of macromolecules. Edited by Hames BD. Oxford university press, OxfordGoogle Scholar
  17. Kuzmic P (2009) DynaFit--a software package for enzymology. Methods Enzymol 467:247–280CrossRefPubMedGoogle Scholar
  18. Makarov DE (2015) Single molecule science: physical principles and models. CRC Press, Boca RatonCrossRefGoogle Scholar
  19. Minton AP (2006) How can biochemical reactions within cells differ from those in test tubes? J Cell Sci 119:2863–2869CrossRefPubMedGoogle Scholar
  20. Motulsky H, Christopoulos A (2004) Fitting models to biological data using linear and nonlinear regression: a practical guide to curve fitting. Oxford University Press, Oxford, UKGoogle Scholar
  21. Pudney CR, Hay S, Levy C, Pang J, Sutcliffe MJ, Leys D, Scrutton NS (2009) Evidence to support the hypothesis that promoting vibrations enhance the rate of an enzyme catalyzed H-tunneling reaction. J Am Chem Soc 131:17072–17073CrossRefPubMedGoogle Scholar
  22. Purich DL (2010) Enzyme kinetics: Catalysis & Control: a reference of theory and best-practice methods. Academic Press, LondonGoogle Scholar
  23. Rule GS, Hitchens TK (2006) Fundamentals of protein NMR spectroscopy. Springer, DordrechtGoogle Scholar
  24. Selvin PR, Ha T (eds) (2008) Single-molecule techniques: a laboratory manual. Cold Spring Harbor Laboratory Press, New YorkGoogle Scholar
  25. Stagno JR, Liu Y, Bhandari YR et al (2017) Structures of riboswitch RNA reaction states by mix-and-inject XFEL serial crystallography. Nature 7636:242–246CrossRefGoogle Scholar
  26. Taylor KB (2002) Enzyme kinetics and mechanisms. Kluwer Academic Publishers, DordrechtGoogle Scholar

Copyright information

© European Biophysical Societies' Association (EBSA) 2018

Authors and Affiliations

  1. 1.Department of Chemistry and BiochemistryUniversity of California Santa CruzSanta CruzUSA

Section editors and affiliations

  • Clive R. Bagshaw
    • 1
  1. 1.Department of Chemistry and BiochemistryUniversity of California at Santa CruzSanta CruzUSA