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Biennial Report 2005-2007 - Saha Institute of Nuclear Physics

Biennial Report 2005-2007 - Saha Institute of Nuclear Physics

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214 <strong>Biennial</strong> <strong>Report</strong> <strong>2005</strong>-07active and structural sites leading to disruption <strong>of</strong> the oligomeric enzyme. It culminates in the loss<strong>of</strong> the enzyme activity. We have demonstrated the colocalization <strong>of</strong> the antibiotic and the enzymein the cytoplasmic region <strong>of</strong> Hep G2 cell, thereby supporting the validity <strong>of</strong> our proposition aboutintracellular mode <strong>of</strong> action <strong>of</strong> these anibiotics.P Grihanjali DeviBP6.1.4.2 Mechanism <strong>of</strong> transcription by T7 RNA polymeraseAs a sequel to our earlier report that the dye, cibacron blue binds to the enzyme at the twobinding sites for GTP we have attempted to locate the binding sites for the substrate GTP. Bymeans <strong>of</strong> isothermal calorimetry and docking calculations we mapped the bindng sites partially andelaborated the binding energetics for the association <strong>of</strong> the dye with the enzyme.Sudipta Pal, Rahul BanrejeeBP6.1.4.3 Effect <strong>of</strong> DNA binding antibiotics upon chromatin structureWe have examined the effect <strong>of</strong> a DNA binding plant alkaloid, sanguinarine, upon the structure<strong>of</strong> chromatin and nucleosome. Like other antibiotics, such as mithramycin and chromomycin, thiscompound induces chromatin aggregation and nucleosomal instability leading to DNA release. Wehave also done extensive thermodynamic studies to understand the energetics <strong>of</strong> their associationwith chromatin and nucleosome. Our objective is to detect thermodynamic signature <strong>of</strong> structuralalterations in chromatin and nucleosome induced by the small DNA-binding molecu:w les.Suman Kalyan Pradhan, Parijat Majumder, TK Kundu, Dipak DasguptaBP6.1.4.4 Self Aggregation <strong>of</strong> the drug MithramycinThe anionic form <strong>of</strong> the aureolic acid antibiotic Mithramycin undergoes self-association to formtetramer via the initial formation <strong>of</strong> dimer from monomer. The notable feature <strong>of</strong> the aggregationis that it is mediated by the carbohydrate moieties in the antibiotic, hitherto unreported for carbohydratecontaining antibiotics.Shibojyoti Lahiri, Parijat Majumder, P Grihanjali Devi, Dipak DasguptaBP6.1.5 Cellular & Molecular Biology6.1.5.1 Study <strong>of</strong> the survival pathways, which lead to the inhibition <strong>of</strong> apoptosis inV79 fibroblasts after environmental stressThis study was initiated in 2001 to investigate the roles <strong>of</strong> MAP kinase family enzymes (ERK, P38MAPK and JNK) , and the PI3 kinase -Akt pathway in the inhibition <strong>of</strong> apoptosis/greater survival

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