A. Sri Rama Koti
Dept. of Chemical Sciences
 
Contact
Office

Room No.204, FTNMR Building
Department of Chemical Sciences
Tata Institute of Fundamental Research
Homi Bhabha Road, Colaba
Mumbai 400 005, INDIA

Phone: +91 22 22782790
Fax: +91 22 22804610/4611
E-Mail: koti@tifr.res.in
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Research Interests
Mechanical forces play a central role in ubiquitous phenomena such as cell-adhesion, tissue organization, and muscle function in multi-cellular organisms. Cell-adhesion is also essential in wound healing, protecting us from microorganisms, and maintaining immunity. Unraveling the molecular mechanism of these important biophysical and mechanochemical (chemistry of single-molecules under a stretching forces) processes is an exciting question in modern cell biology. The key players in cell-adhesion are protein molecules on the cell-surface, which act as mechanosensors and communicate the surrounding dynamic microenvironment with the cell. Hence, studying the mechanical response of these biomolecules would provide a wealth of information about their structure, function, and chemistry. We use state-of-the-aft atomic force microscope (AFM) to probe single molecules. By using this novel technique, we can apply stretching force to a single protein molecule, measure its mechanical response and study protein mechanics. The following are the research interests:
Mechanochemistry (chemistry upon mechanical activation of bonds) and kinetic characterization of chemical and biochemical reactions.
Investigation of mechanical behaviour and functional role of different classes of cell-adhesion biomolecules.
Engineering novel proteins with diverse mechanical functions based on cell-adhesionproteins.
Elucidation of mechanical unfolding/unfolding pathways of proteins and their relation with biochemical pathways.
Development of novel single-molecule assays for protein-protein, protein-DNA, and protein-RNA interactions.

A single-molecule assay to directly identify solvent accessible disulfide bonds and probe their effect on protein folding
J.Amer.Chem.Soc. 130, 436(2008)
 

Counter length and refolding rate of a small protein controlled by engineered disulfide bonds
Biophys. J. 92, 225 (2007)
 

Force-dependent chemical kinetics of disulfide bond reduction observed with single-molecule techniques
Proc. Natl. Acad. Sci. USA 103, 7222 (2006)
 

Mechanical unfolding pathways of the enhanced yellow fluorescent protein revelaed by single molecule force spectroscopy
J. Biol. Chem. 281, 40010 (2006)
 

Ligand binding modulates the mechanical stability of dihydrofolate reductase (DHFR)
Biophys. J. 89, 3337 (2005)