THERMODYNAMIC ANALYSIS OF BIOMOLECULES - A VOLUMETRIC APPROACH

Fundamental thermodynamic relationships reveal that volumetric studies on molecules of interest can yield useful new information. In particu lar, appropriately designed volumetric studies can characterize the pr operties of molecules as a function of solution conditions, including the role of solvation. Until recently, such studies on biologically in teresting molecules have been limited because of the lack of readily a vailable instrumentation with the requisite sensitivity; however, duri ng the past decade, advances in the development of highly sensitive, s mall-volume densimetric, acoustic and high-pressure spectroscopic inst rumentation have enabled biological molecules to be subjected to a wid e range of volumetric studies, In fact, the volumetric methods used in these studies have already provided unique insights into the molecula r origins of the intramolecular and intermolecular recognition events that modulate biomolecular processes. Oi particular note are recent vo lumetric studies on globular proteins and nucleic acid duplexes. These studies have provided unique insights into the role of hydration in m odulating the stabilities of these biopolymers, as well as their confo rmational transitions and ligand-binding properties.