New York, N.Y. - Columbia researchers are making a major contribution to the rapidly expanding field of structural genomics, an endeavor that relates protein structures to the genetic sequences that encode them. The effort may reveal rules that could be used to predict the shape of a protein from its sequence.
Determining the structure of a protein may help explain its function as well as how it may be affected by both normal physiological and pathological processes. Detailed structural information also enables researchers to model a protein's interactions with a drug candidate, greatly aiding in pharmaceutical design. While the Human Genome Project has yielded the sequences of genes for a vast number of proteins, their actual structures have yet to be determined. Therefore, determining the 3-D structure of isolated proteins constitutes an important part of a new structural genomics program funded by National Institute of General Medical Sciences (NIGMS). "The idea is to try to find a large number-ultimately, representative of all different types of sequence." Dr. Wayne Hendrickson, professor of biochemistry and molecular biophysics and leader of the Columbia team, says the goal of the initiative is 10,000 structures in 10 years. "The optimism for being able to do this is based on advances in techniques.
"It's a cross-disciplinary project. The idea is to carry out analysis of protein structure on a pan-genomic scale, bringing together capability in experimental determination of structure and bioinformatics," says Dr. Hendrickson. Columbia faculty involved in the research are professors Barry Honig, Eric Gouaux, Arthur Palmer and Burkhard Rost in biochemistry and molecular biophysics; John Hunt and Liang Tong in biological sciences; Andrew Laine in biomedical engineering; Peter Allen in computer science; and Ann E. McDermott in chemistry, biological sciences, and chemical engineering and applied chemistry.