| Adams,
Michael W. W. |
E-mail:
adams@bmb.uga.edu |
| The
hyperthermophilic archaeon Pyrococcus furiosus (Pf) grows optimally
at 100°C by fermenting peptides and sugars. It also reduces
elemental sulfur to hydrogen sulfide. From Pf we are purifying
and characterizing a range of metal-containing, oxidoreductase-type
enzymes and redox proteins that are involved in unusual catabolic
pathways. In addition, all ORFs in the Pf genome (1.9 Mb) are
being cloned and expressed in an NIH-funded structural genomics
initiative with the goal of obtaining 3D structures on all Pf
proteins. The function of all Pf ORFs are being assessed using
DNA microarrays and proteomic approaches in conjunction with
metabolic and physiological analyses. |
| Keywords:
Archaea, hyperthermophile, metalloenzymes, genomics, microarrays,
proteomics |
|
| Brewer,
John M. |
E-mail:
brewer@bmb.uga.edu |
| I
do site-directed mutagenesis on yeast enolase, changing residues
the X-ray structure indicates are important in the enzyme mechanism
or involved in the interaction between the two subunits. |
| Keywords:
enolase, enolase mechanism, subunit, conformation |
|
| Dailey,
Harry A. |
E-mail:
hdailey@uga.edu |
| Our
research program examines regulation of mammalian heme biosynthesis
in erythroid and non-erythroid cell types from both normal and
porphyric animals. Structure / function studies on a number
of the heme synthetic pathway enzymes are designed to determine
the catalytic mechanism of these proteins and also to understand
the deficiencies that exist in naturally occuring mutants of
these enzymes. |
| Keywords:
Heme biosynthesis, porphyrias, protein structure / function,
regulation, ferrochelatase, human genetic diseases |
|
| 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. |
|
| Moremen,
Kelley W. |
E-mail:
moremen@uga.edu |
| Research
in the Moremen lab focuses on the structure, enzymology, regulation,
and localization of enzymes involved in the biosynthesis, recognition,
and catabolism of mammalian glycoproteins. Carbohydrate structures
on glycoproteins contribute to many biological recognition events
between molecules and between cells in an organism. Alterations
in the synthesis and degradation of these structures can also
occur in human genetic disease. Work in the Moremen lab is focused
on (1) the characterization of enzymes involved in mammalian
glycoprotein biosynthesis and catabolism and the functionally
defective forms of these enzymes involved in human genetic disease
and (2) the identification and characterization of carbohydrate-binding
proteins and their roles in vertebrate development and physiology. |
| Keywords:
enzymology and molecular biology of glycosylation enzymes, enzyme
structure, human genetic disease |
|
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