Dr. Scheraga's group is investigating the interactions that

• Dictate the folding of a polypeptide chain in water into the three-dimensional structure of a native protein and
• Determine the reactivity of such a protein molecule (e.g., as an enzyme) with other small and large molecules.

Both experimental and theoretical methods are used in this research. The experimental work involves 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. 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, and enzyme-substrate complexes. Much of the experimental and theoretical work involves the determination of the pathways of folding of proteins, and the mechanism of action of thrombin on fibrinogen (an important reaction in the blood clotting process).

•             Member, Council, Biophys. Soc., 1967-70

•             Member-at-Large, Council of the Gordon Research Conferences, 1969-71
•             Member, Advisory Panel in Molecular Biology, National Science Foundation, 1960-62
•             Member, Biochemistry Training Comm., National Institutes of Health, 1963-65
•             Member, Research Career Award Comm., NIGMS, National Institutes of Health, 1967-71
•             Ad Hoc Member, BBCA Study Section, NIH, June 1989
•             Member, Technical Advisory Panel, Xerox Corp., 1969-71; 1974-79
•             Member, Board of Governors, Weizmann Institute, Rehovoth, Israel, 1970-1997; Emeritus, 1997-
•             Member, Scientific Advisory Board, Geneformatics, 2000-2003 ; IBM Blue Gene Project, 2001-2003; Buffalo Center of Excellence in Bioinformatics, 2003-2005.
•             Member, Chemistry Dept. Visiting Comm., Brookhaven National Lab., 1972-74; Chairman, 1974
•             Member, Commission on Molec. Biophys., Intntl. Union for Pure and Applied Biophys., 1967-69
•             Member, Commission on Macromolecular Biophys., Intntl. Union for Pure and Applied Biophys., 1969-75; President, 1972-75
•             Member Commission on Subcellular and Macromolecular Biophys., Intntl. Union for Pure and Applied Biophys., 1975-81
•             Representative of IUPAB to Macromolecular Division, IUPAC, 1969-84
•             Representative of IUPAC to International Union of Biochemistry, 1970-73
•             Representative of Amer. Chem. Soc. on U.S. National Committee for IUPAC, 1974-79
•             Member, Am. Chem. Soc., Am. Soc. Biol. Chem., Biophys. Soc., Am. Assoc. Adv. Sci., Phi Beta Kappa, Sigma Xi, Phi Lambda Upsilon, Alpha Chi Sigma

• B.S., City College of New York, 1941
• A.M.(1942) Ph.D. (1946), Duke University

• Fulbright Research Scholar
• National Institutes of Health Special Fellow, Fogarty Scholar
• American Chemical Society: Eli Lilly Award; Kendall Award; Mobil Award; Repligen Award; IBM Award; Hirschmann Award
• Nichols Medal
• Pauling Medal
• Linderstrøm-Lang Medal
• Stein and Moore Award of the Protein Society