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TETRAD FACULTY
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Protein Folding and Drug Design
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The Cohen group is interested in the application of computers, computational simulations and database searches to problems in biology and pharmacology. This work divides into four areas:
Structure-based Drug Design - Our emphasis is on cysteine proteases that play critical roles in the life cycles of parasitic organisms causing Malaria, Chagas disease and Sleeping Sickness. In particular, we are using the tools of structure-based drug design to direct the design and synthesis of non peptidic small molecules that bind in a non covalent fashion to inhibit the relevant enzyme.
Deducing Protein Sequence Structure Functional Relationships - With the success of genome sequencing projects, increasingly the question asked is, "What does a new sequence do?" In this regard, it appears that structure is a useful intermediate in recognizing sequence relationships and the functional connections that are often implied. We are developing computational algorithms that recognize these relationships and strategies to use evolutionarily related sequences and the patterns of sequence variation at the DNA level to expand our ability to detect functionally relevant sites on protein surfaces as well as sequence structure relationships.
Molecular Basis of Prion Diseases - As part of a longstanding collaboration with Stan Prusiner, we are studying the structure and biochemical properties of the prion protein in its normal (PrPc) and disease causing (PrPSc) isoforms. We are interested in the mechanism of prion replication, diagnostic tests that could detect the formation of PrPSc, and in the development of small molecule therapeutics that could block this process.
Design, Synthesis and Characterization of Structured Sequence Specific Heteropolymers Based on the N-alkylated Glycine Backbone - During the past three years we have been interested in the design and synthesis of peptoids, peptide analogs where the R-group is shifted from the Ca to the Nitrogen. When chiral side chains are introduced, these heteropolymers can exhibit a very stable cis polyproline type I-like helical structure. We have synthesized polypeptoids that can bind DNA, protect it from nuclease cleavage, and package the DNA to facilitate cell transfection. We are now interested in creating polypeptoids that adopt unique tertiary structures.
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| Featured paper | | Baf60c is essential for function of BAF chromatin remodelling complexes in heart development.
Bruneau lab | | Download the pdf |
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Faculty
