NMR spectroscopy provides a powerful non-destructive
tool for determining atomic-level structural features and dynamics
of a wide range of molecules, including those comprising only
a few atoms to those as large as 100 Kilodaltons or greater. Structural
information can be obtained for biomacromolecules in solution
under native conditions of pH, ionic strength, and temperature.
Macromolecular interactions can also be readily studied, even
for systems that interact weakly or exist in multiple conformations.
New NMR methods have recently been developed that even allow studies
of protein folding and enzyme reactions as these processes are
actually occurring.
The department has 400 MHz and 500
MHz (with cryoprobe) NMR spectrometers that are available for
departmental use. The Howard Hughes Medical Institute contains
two 600 MHz and one 800 MHz NMR instrument, all equipped with
cryoprobes.
Contact information and more specifics on capabilities and
applications can be found on UMBC's NMR website.
UMBC
Nuclear Magnetic Resonance Facility
