In collaboration with Rutgers scientists, NESG members at Columbia University will have significant roles in the program, including the selection of specific proteins for structure determination and subsequent computational analysis of the structures. From the structures, Columbia bioinformatics specialists will be able to deduce functional information about individual proteins and bring to light new evolutionary relationships among them.
"We hope that the PSI will allow us to develop a new view of the relationships between protein sequence, protein structure and protein function that will ultimately make the three-dimensional structures and functions of most proteins predictable from the protein sequence," said Barry Honig, professor of biochemistry and molecular biophysics at Columbia University Medical Center and bioinformatics leader of the NESG.
Wayne Hendrickson, University Professor of Biochemistry and Molecular Biophysics at Columbia, is participating as NESG's director of crystallography.
"The PSI has transformed protein structure determination into a highly automated process, making it possible to go from a selected target to a completed structure much more rapidly than before," said Jeremy M. Berg, director of NIGMS. "Building on these achievements, the new centers will take the PSI to the next level, yielding large numbers of structures and tackling significant new challenges. Importantly, the technology developed will continue to impact structural studies beyond the PSI."
Montelione expects that in the next five years his group should solve about 1,000 more structures, including many human protein structures, using methods of X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy, with the full PSI producin
Source:Rutgers, the State University of New Jersey