Thermodynamic problems in structural molecular biology*
Peter L. Privalov
Department of Biology, Johns Hopkins University, Baltimore, MD 21218, USA
Abstract: The most essential feature of living biological systems is their high degree of structural organization. The key role is played by two linear heteropolymers, the proteins and nucleic acids. Under environmental conditions close to physiological, these biopolymers are folded into unique native conformations, genetically determined by the arrangement of their standard building blocks. In their native conformation, biological macromolecules recognize their partners and associate with them, forming specific, higher-order complexes, the "molecular machines". Folding of biopolymers into their native conformation and their association with partners is in principle a reversible, thermodynamically driven process. Investigation of the thermodynamics of these basic biological processes has prime importance for understanding the mechanisms of forming these supra-macromolecular constructions and their functioning.
Keywords: microcalorimetry; macromolecules; DNA; proteins; hydration; thermodynamics.
*Paper based on a presentation at the 19th International Conference on Chemical Thermodynamics (ICCT-19), 30 July to 4 August 2006, Boulder, CO, USA. Other presentations are published in this issue, pp. 1345-1462.