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Cell division: We are studying the role played by cytoplasmic membrane
proteins in the process of cell division using techniques of gene
fusion, domain swapping, and immunofluorescence microscopy. We wish
to understand how the formation of a complex structure such as a cell
septum is initiated and propagated. More...
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Protein folding: We are characterizing enzyme systems that
are required for the efficient formation and isomerization of disulfide
bonds in proteins of the bacterial cell envelope. We are studying
1) the source of oxidizing potential for formation and 2) how the
protein which catalyzes disulfide bond formation acts on its substrates.
We study the basis for the finding that cytoplasmic proteins do not
contain disulfide bonds. This has led to characterization of the roles
of the thioredoxin and glutathione-glutaredoxin systems in maintaining
the thiol reducing environment in the cytoplasm. More... |
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Membrane protein structure: We have developed a gene fusion
technique for determining the topology of integral membrane proteins
within the lipid bilayer. We are developing techniques for defining
the interactions between the segments of membrane proteins that are
imbedded in membranes. We hope to develop rules allowing the prediction
of aspects of the structure of a membrane protein from its amino acid
sequence. More... |
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Protein secretion: We have defined a set of sec genes whose
products are part of a machinery required for the process of protein
translocation across the cytoplasmic membrane. We use genetic and
in vitro studies to characterize the role of various components in
this complex process. More... |
