Abstract
The reversible interaction or binding of ligands to biological macromolecules is fundamental to nearly every aspect of biochemistry and cell biology. Binding events typically do not occur in isolation in biochemistry, and are almost always coupled or linked to other reactions such as protonation changes, other ligand-binding interactions, structural transitions, and folding. It is rarely sufficient to simply state that something binds. An understanding of binding requires a measure of affinity, stoichiometry, and the contributions of linked reactions. Emphasis is placed here on defining binding and the influence of linkage on binding and stability using both spectroscopic and calorimetric data.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Notes
- 1.
This work was supported by the National Institutes of Health (GM 49686).
References
Edsall, J. T., Gutreund, H. (1983) Biothermodynamics, John Wiley and Sons, New York.
Conners, K. A. (1987) Binding Constants: The Measurement of Molecular Complex Stability, John Wiley, New York.
Wyman, J., Gill, S. J. (1990) Binding and Linkage: Functional Chemistry of Biological Macromolecules, University Science Books, Mill Valley, CA.
Marshall, A. G. (1978) Biophysical Chemistry, John Wiley & Sons, New York.
Eisenberg, D., Crothers, D. (1979) Physical Chemistry with Applications to the Life Sciences, Benjamin/Cummings, Menlo Park, CA.
Lumry, R., Biltonen, R., Brandts, J. (1966) Validity of the “two-state” hypothesis for conformational transitions of proteins, Biopolymers 4, 917–944.
Biltonen, R. L., Freire, E. (1978) Thermodynamic characterization of conformational states of biological macromolecules using differential scanning calorimetry. CRC Crit Rev Biochem 5, 85–124.
Privalov, P. (1979) Stability of proteins. Small globular proteins. Adv. Protein. Chem. 33, 167–241.
Freire, E. (1995) in (Shirley, B., Ed.) Protein Stability and Folding, Humana Press, Totowa, N.J.
Makhatadze, G., Privalov, P. L. (1995) Energetics of protein structure. Adv Protein Chem 47, 308–425.
Becktel, W., Schellman, J. (1987) Protein stability curves. Biopolymers 26, 1859-1877.
Brandts, J. F., Lin, L.-N. (1990) Study of strong to ultratight protein interactions using differential scanning calorimetry. Biochemistry 29, 6927–6940.
Edsall, J. T., Wyman, J. (1958) Biophysical Chemistry, Academic Press, New York.
Tanford, C. (1970) Protein denaturation. Part C: Theoretical models for the mechanism of denaturation. Adv Protein Chem 24, 1–95.
Perutz, M. F. (1978) Electrostatic effects in proteins. Science 201, 1187–1191.
Honig, B., Nicholls, A. (1995) Classical electrostatics in biology and chemistry. Science 268, 1144–1149.
Yang, A. -S., Honig, B. (1993) On the pH dependence of protein stability. J Mol Biol 231, 459–474.
Garcia-Moreno E. B. (1995) Probing structural and physical basis of protein energetics linked to protons and salt. Meth. Enzymol. 259, 512–538.
Antosiewicz, J., McCammon, J. A., Gilson, M. K. (1996) The determinants of pK as in proteins, Biochemistry 35, 7819–7833.
Baker, B. M., Murphy, K. P. (1996) Evaluation of linked protonation effects in protein binding reactions using isothermal titration calorimetry. Biohphysical J 71, 2049–2055.
McCrary, B. S., Edmondson, S. P., Shriver, J. W. (1996) Hyperthermophile protein folding thermodynamics: Differential scanning calorimetry and chemical denaturation of Sac7d. J Mol Biol 264, 784–805.
McCrary, B. S., Bedell, J., Edmondson, S. P., et al. (1998) Linkage of protonation and anion binding to the folding of Sac7d. J Mol Biol 276, 203–224.
Clark, A., McCrary, B. S., Edmondson, S., et al. (2004) Thermodynamics of core hydrophobicity and packing in the hyperthermophile proteins Sac7d and Sso7d. Biochemistry 43, 2840–2853.
Lakowicz, J. (1999) Principles of Fluorescence Spectroscopy. Springer, New York.
Wiseman, T., Williston, S., Brandts, J. F., et al. (1989) Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal Biochem 179, 131–137.
Breslauer, K. J., Freire, E., Straume, M. (1992) Calorimetry: A tool for DNA and ligand–DNA Studies. Meth Enzymol 211, 533–567.
Bundle, D. R., Sigurskjold, B. W. (1994) Determination of accurate thermodynamics of binding by titration microcalorimetry. Meth Enzymol 247, 288–305.
Lopez, M. M., Makhatadze, G. I. (2002) Isothermal titration calorimetry. Methods Mol Biol 173, 121–126.
Wang, P., Izatt, R. M., Gillespie, S. E., et al. (1995) Thermodynamics of the Interaction of 18-crown-6 with K+, Tl+, Ba+2, Sr+2 and Pb+2 from 323.15 to 398.15 K, J Chem Soc Faraday Trans 91, 4207–4213.
Bevington, P. (1969) Data Reduction and Error Analysis for the Physical Sciences, McGraw-Hill, Inc., New York.
Beechem, J. M. (1992) Global analysis of biochemical and biophysical data. Methods Enzymol 210, 37–54.
Gordon, A., Ford, R. (1972) The Chemist's Companion: A Handbook of Practical Data, Techniques, and References, John Wiley, New York, N.Y.
Acknowledgments
This work was supported by NIH RO1 GM049686.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2009 Humana Press, a part of Springer Science+Business Media, LLC
About this protocol
Cite this protocol
Shriver, J.W., Edmondson, S.P. (2009). Ligand-Binding Interactions and Stability. In: Shriver, J. (eds) Protein Structure, Stability, and Interactions. Methods in Molecular Biology, vol 490. Humana Press. https://doi.org/10.1007/978-1-59745-367-7_6
Download citation
DOI: https://doi.org/10.1007/978-1-59745-367-7_6
Published:
Publisher Name: Humana Press
Print ISBN: 978-1-58829-954-3
Online ISBN: 978-1-59745-367-7
eBook Packages: Springer Protocols