| Lee,
John W. |
E-mail:
jlee@uga.edu |
| The
major research interest is in the biophysical aspects of bioluminescence.
We utilize picosecond fluorescence dynamics and macromolecular
structural methods: high-field nuclear magnetic resonance and
X-ray crystallography. The properties of certain fluorescent
proteins occurring in the bioluminescent bacteria have been
given detailed study, such as spectral properties, primary sequence,
and three-dimensional structure. Current work concentrates on
the calcium-regulated photoproteins, obelin and aequorin. These
studies involve collaborations with groups in Holland and Russia
with support by the Office of Naval Research. |
| Keywords:
bioluminescence, fluorescence, picosecond, bacterial luciferase,
photobacterium, photoprotein, aequorin, obelin, lumazine protein,
NMR, X-ray crystallography. |
|
| Legault,
Pascale |
E-mail:
pascale@bmb.uga.edu |
| The
research in our laboratory focuses on NMR spectroscopy and biochemical
studies of RNAs and RNA-protein complexes in order to gain a
structural understanding of their biological function. Several
ribozymes are currently being investigated to help understand
the structural basis of RNA catalysis. The activity of these
ribozymes depends on specific divalent metals for proper folding
and chemical reactivity. We are determining the structure of
these ribozymes and studying their interaction with divalent
metal ions. Several RNA-protein interactions that play key roles
in HIV infection are also being investigated using binding and
NMR methods. In addition, we are studying the effect of small
organic compounds on these RNA-protein interactions to provide
insights in the design of improved anti-HIV drugs. |
| Keywords:
RNA, RNA-protein interactions, HIV, ribozyme, metal binding,
structural biology, NMR spectroscopy |
|
| Prestegard,
James H. |
E-mail:
jpresteg@ccrc.uga.edu |
| The
Prestegard group applies Nuclear Magnetic Resonance (NMR) spectroscopy
to the investigation of structural and functional properties
of biologically important systems. Systems of interest include
carbohydrate binding proteins, metallo-proteins and membrane
associated proteins. These systems play important roles in cell
signalling, cell differentiation, and cell-cell interaction.
As such, they become targets for rational drug design. NMR provides
a useful tool for these investigations. However, NMR is also
an evolving tool, limited both by current experimental approaches
and data analysis procedures. To push back limits of applicability
the group also devotes considerable effort to method development. |
| Keywords:
NMR, carbohydrates, membrane proteins, structural genomics,
protein structure, protein dynamics, drug design |
|
| York,
William S. |
E-mail:
will@ccrc.uga.edu |
| The
"primary" cell wall, which surrounds growing plant cells, plays
a key role in plant development. One of its most important functions
is to control the rate and orientation of cell expansion. Polysaccharide
networks in the wall expand by gradually yielding under osmotic
stress, allowing the cell to grow in a controlled, oriented
fashion. This process determines the morphology of each cell,
which ultimately determines the shape of the entire plant. Research
in my laboratory is aimed at characterizing the molecular dynamics
and topology that lead to the assembly and controlled expansion
of the cell wall. |
| Keywords:
Plant Cell Walls, Xyloglucan, Polysaccharides, NMR, Molecular
Dynamics, Plant Growth, Self Assembly |
|
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