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Peter C. Kahn
Professor
Rutgers University
Dept. of Biochemistry & Microbiology
328 Lipman Hall
School of Env & Biol Sciences
New Brunswick. NJ 08903
(732) 932-9255, Ext 120
FAX - 8965
kahn@aesop.rutgers.edu |
Protein folding. subunit assembly. ligand interactions. hydration. dioxins
and related compounds
Protein biophysics- We study protein folding and the intermolecular
interactions between protein subunits of multimolecular complexes. between
proteins and small ligands. and between cations and DNA. Particular emphasis
is placed on the role(s) of water of hydration. Among the properties of
hydrating solvent which differ from those of bulk water is the density.
Changes in density manifest as changes in volume. which we measure. along
with a variety of spectroscopic and other properties. Both equilibrium and
kinetic data are obtained. often from the same experiments. In the refolding
of ribonuclease-A. for example. two slow processes are seen which occur
concurrently with different time constants and different kinetic responses
to altered solution conditions. One entails a rise in volume. while the
other yields a fall. Their molecular bases have been tentatively identified.
In a collaborative project we have fused a leader sequence to a globular
protein which is not normal secreted from the cell. The fusion product folds
to the native conformation. but its folding is retarded by the presence
of the leader. with implications for the control both of secretion and for
folding in vivo. Lastly. in theoretical work we have developed methods for
the analysis of protein secondary and tertiary structures which will aid
in protein design and have implications for folding. This last project is
computational and makes heavy use of graphics.
Toxicology and environmental science of dioxins and related compounds- In
a collaborative project we have developed methods to evaluate past exposure
of people to dioxins and related compounds. Studies of Vietnam veterans
exposed to Agent Orange during the war have been completed. We have also
studied environmental exposure of marine animals which feed on contaminated
sediments. the materials through the food chain. Laboratory studies have
focused on purification and identification of proteins which bind dioxin.
For this purpose we have developed an affinity purification column to which
dioxin is covalently attached. An understanding of which proteins may be
involved in dioxin binding will help us understand the broad and somewhat
nonspecific manifestations of the toxicity caused by these compounds.
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