A chemistry symposium in honor of the 75th birthday of Harold Scheraga, Cornell University professor of chemistry emeritus, will be held Saturday, Oct. 19, in Baker Laboratory on the Cornell campus.

Former students, postdoctoral fellows and research colleagues will honor Scheraga's 50 years at Cornell with talks and colloquia on their mentor's favorite area of research -- protein chemistry.

Generations of Cornellians remember Scheraga for his outstanding "protein course," Physical Chemistry of Proteins, and for his general physical chemistry lectures before undergraduate classes. He arrived at Cornell in 1947 after a year at Harvard Medical School as an American Chemical Society Postdoctoral Fellow. Scheraga presided as chairman of a fast-growing chemistry department (1960--67). During his tenure as chairman he oversaw the construction of Olin Laboratory, still known by some as the "new addition" to the department's facilities.

Scheraga was a senior protegŽ of Leo Mandelkern and junior to Cornell Nobel Laureate Paul Flory in early studies of proteins and other polymers, going on to pioneer the development and application of physico-chemical methods to understand interactions in model polypeptides, in proteins, and between enzymes and substrates. He was first to recognize the implications for physical chemistry in the discovery (by Anfinsen) that amino acid sequences dictate the three-dimensional structures of particular proteins.

His contributions to the field are numerous. Scheraga developed a method to interpret the hydrodynamic properties of proteins; his computations of the structure of water and aqueous hydrocarbon solutions showed a physical basis for hydrophobic interactions; he provided an analysis of the helix-coil transition in homo- and copolymers of amino acids, determining the intrinsic helix-forming tendencies of specific amino acids; by ingenious experimentation he determined structurally relevant distance constraints in ribonuclease.

Also, he elucidated the mechanism of the thrombin-induced conversion of fibrinogen to fibrin in blood clotting, leading to his identification of a molecular basis for a specific bleeding disorder; he determined the folding pathways of ribonuclease A; he developed the field of conformational energy calculations on proteins, which has a bearing on his further solution of the multiple-minima problem for oligopeptides, fibrous and globular proteins.

Four of Scheraga's almost 1,000 scholarly papers were designated "citation classics" by Current Contents, and, according to a 1982 issue of the same journal, he is the most frequently cited physical chemist in the world. In 1990, he was considered one of 10 most likely candidates for the Nobel Prize -- the only protein chemist in the list.

Among his awards are the American Chemical Society's Eli Lilly Award in Biochemistry (1957), ACS Kendall Award in Colloid or Surface Chemistry (1978), ACS Pauling Medal (1985), ACS Mobil Award in Polymer Chemistry (1990), ACS Repligen Award for Chemistry of Biological Processes (1990) and the Stein and Moore Award of the Protein Society (1995). He is a member of the National Academy of Sciences (1966) and the American Academy of Arts and Sciences (1967).

In 1965 he was named the George W. and Grace L. Todd Professor of Chemistry, and in 1992 he became Todd Professor Emeritus.

Here is the program schedule for Saturday, Oct. 19 (all events are in Baker Laboratory of Chemistry, Room 200):

• Morning Session, Chairman: Arnie T. Hagler, Molecular Simulations Inc.
• 9 a.m. Opening Remarks
• 9:15 a.m. Jeffrey Skolnick, Scripps Research Institute
• "A Hierarchical Approach to the Prediction of Protein Structure"
• 10 a.m. Break
• 10:30 a.m. Michael Levitt, Stanford University
• "Computer Simulation of Protein Folding and Unfolding"
• 11:15 a.m. Ken Dill, University of California, San Francisco
• "A New Approach to Computing Parttition Functions for
• Biomolecules"
• Afternoon Session
• 2 p.m. Alexander Tulinsky, Michigan State University
• "Molecular Interactions of Thrombin"
• 2:45 p.m. Break
• 3:15 p.m. Walter Englander, University of Pennsylvania
• (no title given)
• 4 p.m. Peter Wright, Scripps Research Institute
• "NMR Characterization of Apomyoglobin Folding Pathways and
• Intermediates"