ISSN: 2161-0398
+44 1478 350008
I. Valpapuram, P. Sonar, M. Caldarini, D. Tavella, C. Volonte, V. Pandini, M. A. Vanoni, A. Aliverti, R. A. Broglia, G. Tiana3 and C. Cecconi
Accepted Abstracts: J Phys Chem Biophys
Understanding protein folding and unfolding of the Human immunodeficiency virus type 1 protease (HIV1-PR) at single molecule level is a challenging mission for both experiments and molecular dynamic (MD) simulations. In the present study, we proposed a novel folding mechanisms using optical tweezers (OT) and MD simulations. Our results confirm that the HIV1-PR reveal multiple pathways through different intermediate on their journey to native state. These include HIV1-PR unfold and refold at high forces. The characterized pathways provide precious information for the design of novel and effective anti-HIV drug.
I. Valpapuram is working as a postdoc at King Abdulla University of Science and Technology (KAUST), KSA. Project: ?Optical tweezers studies of DNA unzipping and replication at single molecule level? June 2013. Postdoc at University of Modena and Reggio Emilia, Italy; Project: ?Energy landscape and inhibition of the folding process of the HIV-1 protease through single molecule manipulation using optical tweezers? 2012-2013. Ph.D. in Physical Sciences at University of Modena and Reggio Emilia, Italy; Thesis: ?Single molecule optical tweezers studies of the unfolding/refolding processes of Acyl-Coenzyme A Binding Protein? 2009-2012. Advance Masters in Nanophysics at the University of Antwerp, Belgium, Thesis: ?Time resolved photoluminescence investigation of charge transfer in organic solar cell materials with novel conjugated polymers? 2008.