Microcalorimetry of Protein-Ligand Interactions
The energetics of enzymic processes and the interactions responsible for protein behaviour have been central to our discussions so far. Several indirect methods are available for probing the thermodynamics of protein interactions, but the most unambiguous and direct experimental approaches are based on calorimetry. Most reactions have an associated heat effect and, apart from its intrinsic interest in terms of energetics, this heat can serve as a useful general probe of biomolecular processes. My purpose here is to describe the basis and applications of isothermal microcalorimetry to the study of interactions at protein binding sites, illustrating the range of information that may be obtained from such studies. But before doing this, we should perhaps consider the nature of the problem and why an empirical, rather than theoretical approach is necessary.
KeywordsTransition State Analogue Calorimetric Enthalpy Isothermal Microcalorimetry Calorimetric Reaction Relative Statistical Factor
Unable to display preview. Download preview PDF.
- Beddell,C.R.,Moult,J. and Phillips,D.C.(1970) in “Ciba Foundation Symposium on Molecular Properties of Drug Receptors”, R.Porter and M.0’Connor, eds., Churchill, London, p.85.Google Scholar
- Cooper,A. and Jenkins,F.M. (1973) in “Protides of the Biological Fluids”, H.Peeters,ed., Pergamon Press, Oxford, p. 457.Google Scholar
- Cooper,A. (1982) Meth.Enzymol., 88: 667.Google Scholar
- Fersht,A. et al.,(1984) Nature, 314:235.Google Scholar
- Sturtevant,J.M. (1962) in “Experimental Thermochemistry”, Vo1.II, H.A.Skinner,ed., Interscience, New York, p. 427.Google Scholar
- Sturtevant,J.M. (1987) Annu.Rev.Phys.Chem., 38:463. Wadso,I.(1974) Pure Appl.Chem., 38: 529.Google Scholar