DISTINGUISHED SCIENTIST LECTURE SERIES AT BARD COLLEGE CONTINUES WITH TALK BY DR. GEORGE D. ROSE, BARD ALUM AND PROFESSOR AT JOHN HOPKINS UNIVERSITY.

ANNANDALE-ON-HUDSON, N.Y.-The Distinguished Scientist Lecture Series at Bard College presents a talk by Dr. George D. Rose, Bard '63, joint-appointed professor of biophysics and biophysical chemistry at John Hopkins University School of Medicine, on Saturday, April 10 at 3:00 p.m. in Olin Hall. Hilton Weiss, the David and Rosalie Rose Distinguished Professor of Natural Sciences and Mathematics at Bard College, will give the prelecture talk at 1:30 p.m. Refreshments will be served between the lectures, which are free and open to the public.

Dr. Rose will speak on "How Proteins Fold: Computer Simulation and Modeling." Dr. Rose is the developer, with Rajgopal Srinvasan (also of John Hopkins), of a computer algorithm LINUS, which predicts the folding and the implied atomic structure of a group of proteins. Recreating protein folding by computer models "has been considered the Holy Grail-the major big theoretical problem that no one thought we would solve in this century, and maybe not in the next," said Nobel laureate Hamilton Smith, professor of molecular biology and genetics at John Hopkins. "This breakthrough puts us light years ahead."

LINUS is an acronym for Local Independently Nucleated Units of Structure, "a conglomerate of words that was carefully crafted to honor the late Linus Pauling, who essentially founded this field," Rose explains. Rose and Srinvasan used their individual gifts to develop LINUS jointly. Srinvasan "wrote the computer program from start to finish," according to Rose. LINUS is built around four basic motifs, and around a discovery that George Rose made in 1979, published in the Journal of Molecular Biology, that protein folding is both local and hierarchical.

The implications of the discovery are not simply abstract but can be applied in practical and necessary ways. With the accurate, almost instantaneous understanding that LINUS provides of the protein structures, proteins can be manipulated and engineered to fit precisely the functional sites of hormones, enzymes, neurotransmitters, and more. Painkillers and antidepressants, for example, can be made both safer and more powerful, because they will be designed to do exactly and only what is wished, with no side effects. Further, says Rose, "an HIV protease could be blocked so that the AIDS virus could not mature." Rose and Srinvasan are currently working on ORF, a program that identifies protein homologs in genomic databases based on comparisons of predicted folded structures.

The long-term possibilities of LINUS are not yet known. A "discovery of this dimension changes the way one sees the world," says Rose, noting, "Nietzsche said that what we see depends on the perspective from which we look. Our very idea of self is called into question by a new worldview. Scientifically and socially, who can say what will arise?"

For further information about the lecture, call 914-758-7508.

This event was last updated on 03-02-2001

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