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Avi
Chakrabartty
Associate Professor
Ph.D., University of Toronto, 1990 |
Ontario
Cancer Institute, MaRS Room 4307
416-581-7553
chakrab@uhnres.utoronto.ca |
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Protein Folding and Design
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Homepage
Research Synopsis
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The highly diverse and complex
three-dimensional (3D) structures of proteins are integral
to their equally diverse and complex functions. The mechanism
by which a particular protein folds into its 3D structure
is encoded in its amino acid sequence. This code is essentially
the second half of the genetic code, and breaking the
code is the ultimate goal of protein folding research.
The protein folding problem is not only a problem of basic
science, but also has important medical applications.
The protein folding code will aid in interpreting genomic
sequences by providing information which can be used to
infer function for new genes. The protein folding code
can also be used to identify the biochemical consequences
of mutations that cause disease. Knowing the protein folding
code is critical for protein design, and the ability to
design proteins will in turn have enormous consequences
for biotechnology.
Our research efforts concentrate on elucidating the mechanism
of protein folding and applying the mechanistic information
to medical problems. Two medical aspects of protein folding
in which we are currently interested include: a) Amyloid
fibril formation and b) Design of polypeptide mimics of
helical cytokines.
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Selected Publications
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S. Bagby, S. Go, S. Inouye,
M. Ikura, and A. Chakrabartty. 1998. Equilibrium folding
intermediates of a greek key beta-barrel protein. J.
Mol. Biol. 276: 669-681.
T.H.J. Huang, P.E. Fraser, and A. Chakrabartty. 1997.
Fibrillogenesis of Alzheimer beta-Amyloid Peptides Studied
by Fluorescence Energy Transfer. J. Mol Biol. 269:
214-224.
J. McLaurin and A. Chakrabartty. 1996. Membrane Disruption
byAlzhemier beta-Amyloid Peptides Mediated Through Specific
Binding to either Phospholipids or Gangliosides: Implications
for Neurotoxicity. J. Biol. Chem. 271: 26482-26489.
Chakrabartty, A., Doig, A.J.,and Baldwin, R.L. 1993. Helix
Capping Propensities in Peptides Parallel Those Found
in Proteins. Proc. Natl. Acad. Sci. USA 90:
11332-11336.
Chakrabartty, A., Schellman, J.A., and Baldwin, R.L. 1991.
"Large Differences Between the Helix Propensities
of Alanine and Glycine". Nature 351:
586-588. |
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