City College of CUNY
Department of Chemistry
Biochemistry Seminar
Wednesday, March 8, 2000
Room J1027
11:15 AM
Stanley Opella
Professor of Chemistry
University of Pennsylvania
NMR Spectroscopy and
Functional Genomics
The structures of individual proteins and their complexes with small
molecules, peptides, and nucleotides are being determined at an
increasingly rapid rate. However, most biological functions are carried
out in a coordinated fashion by groups of proteins from a single operon
or large complexes organized as supramolecular structures, such as
membranes or viruses. As a result, the structures of only a fraction of
the proteins can be solved using currently available high throughput
methods. Only in exceedingly rare cases will all the structural and
regulatory proteins of an operon or virus crystallize in forms suitable
for x-ray diffraction or reorient rapidly in solution for NMR approaches.
Further, proteins in complexes typically are not soluble or, if they are
soluble, don't reorient rapidly in aqueous solution. Fortunately,
solution NMR methods can be adapted and solid-state NMR methods are well
suited for studies of slowly reorienting, immobile or insoluble
molecules. Examples of how NMR can be used to characterize the structures
and dynamics of many proteins found, or soon to be discovered, in the
course of sequencing genomes will be discussed.