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Adithya Polasa
Biography
Adithya Polasa is third year Ph.D. student at University of Arkansas. His doctoral research investigates structure, function, and the mechanism of proteins, as well as molecular dynamics simulation of interactions between metal ions and protein/nucleic acid, and computer aided drug-protein interaction study. His simple pleasures in life include hiking, camping or a run.
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Research
Membrane protein insertase
The capacity to transport proteins from their site of synthesis to their site of capacity is basic for prokaryotic and eukaryotic cells and includes generally saved protein apparatuses that can transport a wide assortment of potential substrates. The YidC/Oxa1/Alb3 group of membrane proteins capacities to embed and intercede the correct collapsing of approaching peptides in the membrane.Membrane proteins should be appropriately embedded and collapsed in the film to be utilitarian.The Escherichia coli Sec translocon and the YidC insertase are engaged with the inclusion of the majority of membrane proteins into the film.YidC intervenes membrane protein insertion and addition in microscopic organisms.It completes its capacity either independently as a membrane insertase or as a chaperone in the SecYEG complex. Notwithstanding its part as an insertase, YidC can likewise go about as a foldase for a few proteins, for example, the sugar transporter LacY and intervene the correct get together of layer protein complexes, for example, the MalFGK2 maltose transporter and the MscL homopentameric pore. The YidC proteins from Gram-negative microscopic organisms have an extra TM helix, which works as a flag arrangement, and a substantial periplasmic area that just from the N-ends of the center transmembrane helices. Despite the fact that the outermembrane domain isn't basic for the YidC function it associates with different segments of the Sec apparatus and is considered to encourage stable complex development. We are investigating the structural dynamics and functutional properties of the YidC in Escherichia coli.
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Mechanosensitive channel of large conductance
Mechanosensitive (MS) channels detect and respond to changes in the pressure profile of cellular membranes and transduce the mechanical energy into electrical and/or chemical signals.
By re-engineering, however, the activation of some MS channels can be triggered by chemical signals such as pH change.
Here, for the first time, we have elucidated the activation mechanism of an engineered MscL channel at an atomic level through a combination of equilibrium, non-equilibrium, biased, and unbiased molecular dynamics (MD) simulations. Comparing the wild-type and engineered MscL activation processes at the atomic level suggests that the two systems are likely to be associated with different active states and different transition pathways.
Peptide-directed nanoparticles study
Nanoparticle synthesized or assembled using various peptides have optimized properties and functional abilities, which can achieve via peptide flexibility and site specificity. Using peptide Pd4 and other alanine substitution combinations of Pd4 attached to green fluorescent protein (GFPuv), we can produce nanoparticles with well-defined sizes that can be soluble in aqueous solutions.
Copyright © 2015, Biomolecular Simulations Group, Department of Chemistry and Biochemistry, University of Arkansas.
These materials are not endorsed, approved, sponsored, or provided by or on behalf of the University of Arkansas, Fayetteville.
For more information, please contact moradi@uark.edu
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