We are interested in physical principles of the architecture of biological macromolecules, proteins, nucleic acids and their complexes. This includes understanding of the energetic basis of these molecular structures, of the forces responsible for folding of polymeric molecules in aqueous media into unique three-dimensional structures and their association with the partner. Recognition of the partners and changes resulting from their interaction is actually the most fundamental biological function displayed on the molecular level. Solution of the above problems requires experimental studies of the changes of biological macromolecules, their mutants and synthetic analogs induced by various external conditions, or by association with the partners and ligands. These processes are studied by various physical methods, and first of all by calorimetry, which provides direct information on the energies involved in the observed processes. The heat effects of intra- and inter-molecular processes studied in dilute solutions are usually extremely small. Therefore to measure these effects we had to develop special supersensitive microcalorimetric methods which are widely used now all over the world. The methodology of our research consists of finding correlations between the obtained structural and energetic information, computer simulation of the studied processes, design of synthetic models and their experimental verification. - Privalov, P.L. 1979. Stability of proteins. Small globular proteins. Adv. Protein Chem. 33:167-2044.
- Privalov, P.L. 1982. Stability of proteins. Proteins which do not present a single cooperative system. Adv. Protein Chem. 35:1-104.
- Privalov, P.L. 1989. Thermodynamic problems of protein structure. Annu. Rev. Biophys. Biophys. Chem. 18:47-69.
- Privalov, P.L. 1990. Cold denaturation of proteins. CRC Crit. Rev. Biochem. Mol. Biol. 25:281-305.
- Privalov, P.L. 1992. Physical basis of the stability of the folded conformations of proteins. In Protein folding, ed. T.E. Creighton, 83-126. New York: Freeman and Co.
- Makhatadze, G.I., and P.L. Privalov. 1995. Energetics of protein structure. Adv. Protein Chem. 47:307-309.
- Privalov, P.L. 1996. Intermediate states in protein folding. J. Mol. Biol. 259:707-725. Wintrode, P.L., and P.L. Privalov. 1997. Energetics of target peptide recognition by calmodulin. J. Mol. Biol. 273:1048-1060.
- Tamura, A., and P.L. Privalov. 1997. The entropy cost of protein association. J. Mol. Biol. 273:1048-1060.
- Privalov, P.L. 1999. Protein stability. In Encyclopedia of Molecular Biology, ed. T. Creighton, 2016-2020. New York: Wiley. Privalov, P.L. 1999. Unfolded proteins. In Encyclopedia of Molecular Biology, ed. T. Creighton, 2723-2725. New York: Wiley.
- Privalov, G.P., and P.L. Privalov. 1999. Problems and prospects in the microcalorimetry of biological macromolecules. Methods Enzymol. 323:31-62.
- Privalov, P.L. 1999. Forces stabilizing protein structure. In Perspectives in Structural Biology. A volume in honor of G.N. Ramachandran, eds. M. Vijayan, N. Yathindra, and A.S. Kolaskar, 449-466. Hyderabad, India: Universities Press (India) Ltd.
- Privalov, P.L., I. Jelesarov, C.M. Read, A.I. Dragan, and C. Crane-Robinson. 1999. The energetics of HMG box interactions with DNA. Thermodynamics of the DNA bonding of the HMG box from mouse sox-5. J. Mol. Biol. 294:997-1013.
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