Avi Chakrabartty

Avi Chakrabartty

Associate Professor

Address MaRS Centre
Toronto Medical Discovery Tower
4th Floor Room 4-307
101 College St.
Toronto, ON M5G 1L7
Lab Chakrabartty Lab
Office Phone 416-581-7553
Email chakrab@uhnres.utoronto.ca

Research Lab

Learn more: Chakrabartty Lab

Research Description

Protein Folding and Design

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.


View all publications on PubMed

Binding of TDP-43 to the 3'UTR of its cognate mRNA enhances its solubility.
Sun Y, Arslan PE, Won A, Yip CM, Chakrabartty A.
Biochemistry. 2014 Sep 23;53(37):5885-94  Read

Protein misfolding in the late-onset neurodegenerative diseases: common themes and the unique case of amyotrophic lateral sclerosis.
Mulligan VK, Chakrabartty A.
Proteins. 2013 Aug;81(8):1285-303.  Read

Early steps in oxidation-induced SOD1 misfolding: implications for non-amyloid protein aggregation in familial ALS.
Mulligan VK, Kerman A, Laister RC, Sharda PR, Arslan PE, Chakrabartty A.
J Mol Biol. 2012 Aug 24;421(4-5):631-52.  Read