WILLIAM H. STEIN MEMORIAL LECTURE

Rescuing the Conformation of Tumor Suppressor p53

Sir Alan Roy Fersht, Ph.D.
Herchel Smith Professor of Organic Chemistry
Director, Cambridge Centre for Protein Engineering, University of Cambridge

DATE: Friday, February 28, 2003
3:15 p.m. Tea
3:45 p.m. Lecture
PLACE:

Caspary Auditorium
The Rockefeller University
York Avenue at East 66th Street
New York City

Alan Fersht combines the methods of chemistry with those of molecular biology for studying complex problems at the interface of chemistry and biology. In particular, he works in the general area of the structure, activity, stability, folding and design of proteins, and the role of protein misfolding and instability in cancer and disease. He was the first to apply site-directed mutagenesis to analyze the structure and activity of proteins and the strength and specificity of protein interactions, and is one of the founders of protein engineering.

Fersht’s current work focuses on two specific areas. The first is in elucidating at atomic resolution how proteins fold and unfold, using advanced structural and biophysical methods on engineered proteins. His method of phi-value analysis of mutated proteins is now the standard procedure for characterizing experimentally transition states for protein folding and unfolding, and benchmarking simulation at atomic resolution. The second is using the same biophysical methods to study how mutation affects proteins in the cell cycle, particularly the tumor suppressor p53, to design novel anti-cancer drugs that function by restoring the activity of mutated proteins.

A fellow of the Royal Society, Fersht also is a foreign associate of the U.S. National Academy of Sciences, honorary foreign member of the American Academy of Arts and Sciences, and a member of EMBO and Academia Europaea. He was knighted in 2003 for his work on protein science.

He has won several international awards, including: the FEBS Anniversary Prize, Jerusalem, 1980; Novo Biotechnology Award, 1986; Charmian Medal of the Royal Society of Chemistry, 1986 (for Enzymology); The Gabor Medal of the Royal Society, 1991 (for Molecular Biology); Max Tishler Lecture and Prize, Harvard University, 1992; FEBS Datta Lecture and Medal, 1993; Jubilee Lecture and Harden Medal of the Biochemical Society, 1993; the Feldberg Foundation Prize, 1996; Distinguished Service Award (for Protein Engineering), Miami Nature Biotechnology Winter Symposium, 1997; the Davy Medal of the Royal Society, 1998 (for Chemistry); the Chaire Bruylants, 1999; Natural Products Award of the Royal Society of Chemistry, 1999; and the Anfinsenp (1999) and Stein and Moore (2001) awards of the Protein Society.

Admission is free. No registration is required.

For more information, please call Ms. Gloria Phipps at (212) 327-8967.




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