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Biennial Report 2005-2007 - Saha Institute of Nuclear Physics

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206 <strong>Biennial</strong> <strong>Report</strong> <strong>2005</strong>-07Fig.6.1.2.1. Ribbon model <strong>of</strong> LdCyp showing active site residuesL.donovani adenosine kinase (LdAdK) and Arg147 in LdCyp was found to play a key role inreactivating LdAdk. Cyclophilin mutant (R147A) has been crystallized and also the molecularbiology <strong>of</strong> calcineurin and some other proteins has been initiated.V Venugopal, Banibrata Sen†, Alok K Datta†, Rahul BanerjeeC&MB6.1.2.2 Sequencing, cloning and expression <strong>of</strong> the most thermostable Ervatamin,Ervatamin-COur previous studies on Ervatamins established that Ervatamin-C shows unusual stability amongErvatamins and other related proteases. On the basis <strong>of</strong> this observation we have initiated this programprimarily to understand the role <strong>of</strong> individual amino acid residues to maintain the structuralintegrity <strong>of</strong> the thermostable protein at the molecular level. We have sequenced the Ervatamin-CcDNA and cloned the cDNA in the expression vector.Raka Ghosh, JK Dattagupta, Sampa BiswasC&MB6.1.2.3 Structure-function correlation <strong>of</strong> Cysteine proteases from the latex <strong>of</strong> a medicinalplant Ervatamia coronariaErvatamin-A, -B and -C, three papain-like cysteine proteases have been isolated from the latex <strong>of</strong>the plant, characterized and X-ray structures <strong>of</strong> the three have been solved in the previous years.The thermal stability <strong>of</strong> the individual proteases have been determined from temperature inducedCD spectra and compared among themselves and with other members <strong>of</strong> the family. The structural

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