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Date: May 3, 1999
Conference to Address Problem of Protein Folding
Tantalyzing Problem Has Implications for Drug Design and Genomics Research
PRINCETON, N.J. -- A conference at Princeton May 7-9 will address a tantalizing problem that cuts across the fields of biology, medicine and mathematics: how proteins fold. The conference, titled "Optimization in Computational and Chemistry and Molecular Biology: Local and Global Approaches," will bring together leading scientists who are attempting to solve the problem using mathematics, rather than conventional experimental techniques.
Since the discovery of the structure of DNA in 1953, scientists have mapped out in detail how the genetic blueprint gets translated into proteins, the building blocks of all living organisms. But understanding the makeup of proteins is only half the story. After they are created, proteins fold into intricate shapes that determine how they function. The process of folding is complex. Scientists have not been able to figure out how it happens, why one chemical composition leads to a particular fold.
"It is a fascinating problem because nature does it so quickly and efficiently, and we all fail to predict it," says Professor of Chemical Engineering Christodoulos Floudas, who is co-organizing the meeting.
The payoff for finding a solution could be enormous. The Human Genome Project is flooding scientists with information about the sequences of human genes, but is not yielding nearly as much information about how those genes encode protein structure. The ability to predict the folding pattern of a protein simply by knowing the sequence of the gene that creates it could vastly speed up the development of drugs and the understanding of many diseases.
One approach to solving the problem is a mathematical technique called optimization. It's a process of looking at complex situations that are affected by many variables and understanding what arrangement of variables will produce the desired result. For example, transportation engineers could use optimization to create the most efficient traffic flow on a set of city streets.
Proteins are made up of 20 smaller chemical blocks called amino acids. A typical protein might be made of hundreds of amino acids. But for the purposes of studying protein folding, scientists often look at relatively short oligopeptides or polypeptides. Even a pentapeptide, a protein with just five amino acids, could fold in any of 100 billion possible ways, says Floudas. "How do you develop accurate mathematical models that capture all the interactions?" he asks.
The conference will feature presentations by dozens of research groups from around the world. Three speakers will deliver plenary lectures: Harold Scheraga of Cornell University; Kenneth Dill of the University of California at San Francisco; and Michael Levitt of Stanford University. In addition to the folding question, scientists will address related issues: molecular and peptide docking, nuclear magnetic resonance structure refinement, molecular modeling and dynamics, distance geometry and drug design.
The conference begins each day at 8:20 a.m. and will take place in Auditorium 104 of the Computer Science Building on the Princeton campus. For a schedule of talks and other information about the conference, please see its website at: http://titan.princeton.edu/Conference/main.html.