Assistant Professor of Biochemistry & Molecular Biology
PO Box 980614
Richmond, VA 23298-0614
Email: jscarsdale@hsc.vcu.edu
Telephone: 804-828-7147
Education
- Ph.D., Chemistry, Yale University, 1989.
- B.S., Chemistry, University of Arkansas, 1982
Research
My research interests center on the use of a combination
of multi-dimensional NMR techniques and theoretical
molecular structure calculations to investigate the
solution conformation of biological macromolecules.
High resolution NMR is currently the only technique
that can provide detailed information on the solution
conformation of biological macromolecules. Much of
this information is provided by distance constraints
that are derived from the ratio of cross peak intensities
in cross relaxation correlated experiments, which
serve to elucidate connectivities between pairs of
protons that are spatially proximate. In general,
it is not possible to determine an adequate number
of independent distant constraints to permit the
unambiguous from NMR distance constraint data alone.
Theoretical molecular structure calculations give
rise to a number of energetically similar minimum
energy structures that cannot be distinguished on
the basis of energies alone, given the limited accuracy
of the empirical potential energy functions used
in these calculations. In combination, however, an
accurate structural definition may arise. Potential
energy calculations, on the one hand, serve to exclude
energetically unreasonable structural solutions,
while NMR distance constrants, on the other hand,
serve to select between energetically similar minimum
energy structures.
We are currently applying this combination of techniques
in order to probe the structural basis for a number
of biochemical phenomena. In collaboration with the
group of Dr. R. K. Yu, we are conducting detailed studies
of the solution conformation of cell surface glycoconjugates,
a class of molecules which have been implicated in
a wide variety of biological recognition phenomena,
including antigen-antibody interactions, and in cellular
recognition phenomena is the binding of a protein ligand
to the oligosaccharide. Therefore, we are interested
in studying the solution conformation of a number of
oligosaccharide binding proteins, and the conformational
perturbations in these proteins which are associated
with binding to an oligosaccharide receptor.Currently,
we are concentrating on structural studies on the b-subunit
of cholera toxin and on studying its interactions with
the oligosaccharide moiety of ganglioside GM1, which
is thought to serve as a surface receptor for cholera
toxin.
Publications
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