Scheraga Group Homepage
Professor
Harold A. Scheraga
George W. and Grace L. Todd Professor of Chemistry, Emeritus
Baker Laboratory of Chemistry and Chemical Biology
Cornell University
Ithaca NY 14853-1301
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Research Description
We are investigating the interactions that
(a) dictate the folding of a polypeptide chain in water into the
three-dimensional structure of a native protein and (b) determine the
reactivity of such a protein molecule (e.g., as an enzyme) with other small and
large molecules.
Previously, experimental and theoretical
methods were used in this research, but the current research is confined to the
theoretical approach. The experimental work involved genetic engineering and
hydrodynamic (e.g., sedimentation and viscosity), spectroscopic (Raman,
infrared, fluorescence, nuclear magnetic resonance, electron spin resonance,
ultraviolet absorption, circular dichroism, and optical rotatory dispersion),
immunochemical, and other physicochemical measurements on proteins, synthetic
polymers of amino acids, and model compounds, in studies of the pathways of
protein folding, and the mechanism of action of thrombin on fibrinogen (an
important reaction in the blood clotting process. The theoretical work involves
statistical mechanical studies of aqueous solutions of amino acids and
peptides, and of conformational changes in proteins and polypeptides, and
empirical energy calculations to determine the stable conformations of
proteins, polypeptides, enzyme-substrate complexes, protein-protein
interactions, nucleic acids, protein-nucleic acid interactions, and the
pathways and thermodynamics of folding of proteins. The simulations involve massively parallel
software development and massively parallel computing (with more than 1000
cores).