1975 Dr. Corwin Hansch, Pomona College

The 1975 Tolman Award Medalist
Dr. Corwin Hansch
Carnegie Professor of Chemistry
Pomona College

Dr. Corwin Hansch is a native of North Dakota. He received his B.S. at the University of Illinois and his Ph.D. at New York University. He returned to the University of Illinois as a Merrell Postdoctoral Fellow for a period of six months and then joined the Manhattan Project first at the University of Chicago as a Research Chemist and then at Du Pont as a Group Leader. After the close of the Manhattan Project, Dr. Hansch remained at Du Pont until his appointment at Pomona College in February 1946 where has has risen in the various ranks now to the hold the Carnegie Professorship in Chemistry.

Dr. Hansch is the author of 150 publications and co-author with George Helmkamp of the widely used text entitled “Organic Chemistry”. This is now in its third edition including a Spanish translation. Dr. Hansch is a member of several honorary societies and has been previously recognized in several ways for his achievements. In 1975 he received the ACS Smissman Award in Medicinal Chemistry for his work toward the correlation of biological activity with chemical structure. In 1969, he received the Manufacturing Chemists’ Association Award for Teaching of College Chemistry as well as the American Pharmaceutical Association’s Research Achievement Award in Pharmaceutical and Medicinal Chemistry. In 1967, he received the Medal of the Italian Society of Pharmaceutical Science.

Dr. Hansch carries the unusual distinction of having no less than 31 undergraduates as co-authors on one or more published papers. Many of those students are now pursuing active and distinguished careers in the field of chemistry.

Sixteenth Richard C. Tolman Award Meeting
Wednesday, April 21, 1976
Mistele’s Engineers Club

611 W. 6th Street
Los Angeles, CA

1975 Tolman Award Recipient
Dr. Corwin Hansch
Pomona College

“On Enzyme-Ligand Interactions”

Abstract: The understanding of how enzymes bind substrates and inhibitors is one of general importance in biochemistry and molecular biology. Control of enzymic processes via inhibitors is becoming of increasing importance in drug research. Moreover, insight gained from studying the interaction of small organic compounds with purified enzymes in vitro will help in understanding the interaction of drugs with in vivo receptor sites which in general cannot be isolated. We have found that regression analysis can be employed to delineate the relative importance of electronic hydrophobic and steric properties of ligands in their interactions with macromolecules. A discussion of our results with papain and dihydrofolate reductase will be given.