title: Thermodynamic analysis of biomolecular interactions.
abstract: Direct measurement of the thermodynamics of biomolecular interactions is now relatively easy. Interpretation of these thermodynamics in simple molecular terms is not. Recent work shows how the multiplicity of weak noncovalent interactions, and the inevitable enthalpy/entropy compensation that these interactions engender, lead to difficulties in teasing out the different components.
authors.affiliation: Chemistry Department, Glasgow University Glasgow, G12 8QQ, UK. alanc@chem.gla.ac.uk.
authors.forename: A
authors.initials: A
authors.lastname: Cooper
mesh_terms: D000818:Animals; D006801:Humans; D008024:Ligands; D008956:Models, Chemical; D009696:Nucleic Acids / Q000378:metabolism*; D011485:Protein Binding; D017510:Protein Folding; D013816:Thermodynamics
chemical_list: D008024:Ligands; D009696:Nucleic Acids