Peter

Biography

Physical basis of the structure of biological molecules and their complexes From the very beginning of my scientific career, my research interests have concentrated on the physical principles of the architecture of biological macromolecules, proteins, nucleic acids and their complexes, namely the energetics of formation of their unique three-dimensional structures. These aims require experimental studies of the conformation of these molecules under various conditions and measurements of the energies involved in changes of their structures and of their association with molecular partners. The problem of molecular recognition, particularly of DNA by gene regulating proteins, attracts at the present time rapidly increasing attention. Its solution largely depends on the extent of information concerning the energetics of this process. Realization of this program has required development of a supersensitive calorimetric technique, microcalorimetry, which is now widely used in many other laboratories. Except microcalorimetry we are also using extensively various optical methods: CD, fluorescence anisotropy and florescence resonance energy transfer (FRET) to investigate the protein interaction with and changes in their structure resulted from their association.

Research Interest

Physical basis of the structure of biological molecules and their complexes From the very beginning of my scientific career, my research interests have concentrated on the physical principles of the architecture of biological macromolecules, proteins, nucleic acids and their complexes, namely the energetics of formation of their unique three-dimensional structures. These aims require experimental studies of the conformation of these molecules under various conditions and measurements of the energies involved in changes of their structures and of their association with molecular partners. The problem of molecular recognition, particularly of DNA by gene regulating proteins, attracts at the present time rapidly increasing attention. Its solution largely depends on the extent of information concerning the energetics of this process. Realization of this program has required development of a supersensitive calorimetric technique, microcalorimetry, which is now widely used in many other laboratories. Except microcalorimetry we are also using extensively various optical methods: CD, fluorescence anisotropy and florescence resonance energy transfer (FRET) to investigate the protein interaction with and changes in their structure resulted from their association.