Muraleedhara Reddy T

After my graduate studies, I am joined as a M. Phil (2003-2006) student and worked on “in vitro regeneration and biochemical studies on Rue”. Further, I am continuing my research in sequence analysis and structural studies of infectious diseases caused by bacteria and viruses to humans were led to Ph.D (2006-2011) on “in silicon studies of important drug targeted proteins” in bacteria, viruses. In addition, as a senior research fellow I am involved in finding out the mechanism in the sponge tissue formation in mango by enzymatic, radiotracer, HPLC, ELISA and GC-MS. In 2011 June, I was selected as a DBT-Research associate and worked under the guidance of Prof. K. Suguna (Molecular Biophysics Unit, Indian Institute of Science, Bangalore) for more than five years. As a research associate, I have carried out work on cytosolic, periplasmic and membrane protein expression, purification and characterization of proteases like aspartic proteases from Oryza sativa var japonica, Retroviral like proteases from parasitic protozoan organisms and metalloprotease (HtpX) from Mycobacterium tuberculosis strain H37Rv. All O.Sativa APs were showed autoproteolytic activity and proteolytic activity with BSA on acidic conditions. But in the presence of pepstatin A, both catalytic activities were not observed in these proteins. In addition to this, I have expressed Toxoplasma gondii ME49 APs. Like APs, Aspartyl protease of Plasmodium falciparam which is more similar to HIV aspartyl protease. The retroviral protease-like domain is part of a protein called Ddi1 be a potential drug target. I have tried crystallization of full length of DDi1 & Ddi1 domain from P.falciparum 7G8. The purified proteins further mass (KDa) conformed by MALDI-TOF, LC-MS ESI ion trap and LC-MS ESI QTOF. HtpX are difficult to express because of the less solubility of membrane protein and the protein incorporation into the membrane of the host organism. Even though, I have purified HtpX from M. tuberculosis H37Rv.