Wednesday July 27/2:00/Grande Ballroom

Invited Presentation 8

Chair: Giles Auchmuty, University of Houston

Sobering Lessons from a Simple Protein Folding Model

Protein molecules are distinguished by their amino sequences. The "protein folding problem", important to molecular biology and to the pharmaceutical industry, concerns prediction of a protein's preferred three-dimensional folding pattern from that amino acide sequence. To clarify the basic chemical and physical phenomena involved, an elementary "toy model" for protein folding has been invented, incorporating only two "amino acides". Lowest-energy folding patterns have been determined for selected model proteins, yielding a database with a wide variety of folded shapes. Neural networks and other analytical tools have been used to examine the results. The conclusion is that protein folding entails a more complex cooperative character than current theories acknowledge.

Frank H. Stillinger, AT&T Bell Laboratories

Frank H. Stillinger is a Member of Technical Staff in the Materials Chemistry Research Department at AT&T Bell Laboratories, Murray Hill, New Jersey.

Since joining AT&T in 1959 he has been involved in basic research on the molecular nature of water and aqueous solutions, and on phase transitions. His recent work concerns the general theory of structure and dynamics of condensed phases. He has published over 200 articles on statistical mechanics, quantum theory and theoretical chemistry.

Dr. Stillinger was elected a Member of the National Academy of Sciences in 1984, and is a Fellow of the American Physical Society, and has served as Chairman of the Chemical Physics Division of the Society. He was awarded the Elliott Cresson Medal of the Franklin Institute in 1978 for his research on the molecular nature of liquid water and aqueous solutions; the Joel Hildebrand Prize by the American Chemical Society in 1986 for his basic research on liquids. In addition, he received the 1989 Langmuir Award from the American Physical Society.

He received his B.S. degree from the University of Rochester in 1955 and his Ph.D. from Yale University in 1958, both in chemistry.