A Gopala Krishna

A Gopala Krishna

Ph.D, University of Pune
M.Sc, Annamalai University
Office: BT 302
Tel: +91-44-2257-4112
Email: agk@iitm·ac·in
Lab: BT 308

Lab Website

Research Interests

  • G-Protein Coupled Receptor (GPCR) mediated signal transduction pathways
  • Mechanism of G protein activation
  • Membrane protein biochemistry
  • Protein structure-function
  • Protein folding


  1. Sharma, Y., Rao, C. M., Narasu, M.L., Rao, S. C., Somasundaram, T., Krishna, A. G., & Balasubramanian, D.
    Calcium ion binding to crystallins: the presence of the EF-hand motif in crystallin that aids in calcium ion binding.
    J. Biol. Chem. 264: 12794-12799 (1989).
  2. Sharma, Y., Rao, C. M., Rao, S.C., Krishna, A. G., Somasundaram, T. and Balasubramanian, D.
    Binding site conformation dictates the color of the dye Stains-all: A study of the binding of this dye to the eye lens proteins crystallins.
    J. Biol. Chem. 264: 20923-20927 (1989).
  3. Krishna, A. G., & Sharma, Y.
    Conformation of alginate and pectate chains monitored by the binding of the dye Stains-all.
    Ind. J. Biochem. Biophys. 28: 30-33 (1991).
  4. Sharma, Y., Krishna, A. G., & Balasubramanian. D.
    Alteration of the dynamic quaternary structure and calcium-binding ability of ?-crystallin by light.
    Photochem. Photobiol. 57: 739-743 (1993).
  5. Sharma, Y., Krishna, A. G., Balasubramanian, D., Fairwell, T. & Krishna, G.
    Studies on the interaction of the dye, Stains-all, with individual calcium binding domains of Calmodulin.
    FEBS Letters 326: 59-64 (1993).
  6. Krishna, A. G., Balasubramanian, D. & Ganesh, K. N.
    Sugar-DNA molecular recognition: Specific interaction of alpha (1,4) glucopyranose chains with DNA in the minor groove.
    Biochem. Biophys. Res. Comm. 202: 204-210 (1994).
  7. Krishna, A. G.,* Kumar, D. V., Khan, B. M., Rawal, S. K. & Ganesh, K. N.
    Taxol-DNA Interaction: fluorescence and CD studies of the groove binding properties of taxol.
    Biochim. Biophys. Acta 1382: 104-112 (1998). * Corresponding Author.
  8. Marin, E. P., Krishna, A. G., Zvyaga, T. A., Isele. J., Seibert, F. & Sakmar, T. P.
    The amino terminus of the fourth cytoplasmic loop of rhodopsin modulates rhodopsin-transducin interaction.
    J. Biol. Chem. 275: 1930-1936 (2000).
  9. Marin, E. P., Krishna, A. G., Archambault. V., Simuni. E., Fu. W-Y. & Sakmar, T. P.
    The function of interdomain interactions in controlling nucleotide exchange rates in transducin.
    J. Biol. Chem. 276: 23873-23880 (2001).
  10. Marin, E. P., Krishna, A. G. & Sakmar, T. P.
    Rapid activation of transducin by mutations distant from the nucleotide-binding site.
    J. Biol. Chem. 276: 27400-27405 (2001).
  11. Lehmann, N., Krishna, A. G. and Fahmy K
    Suramin affects coupling of rhodopsin to transducin.
    Biophys. J. 82: 793-802 (2002).
  12. Marin, E. P., Krishna, A. G. & Sakmar, T. P.
    Disruption of the ?5 helix of transducin impairs rhodopsin-catalyzed nucleotide exchange.
    Biochemistry. 41: 6988-6994 (2002).
  13. Krishna, A. G., Menon, S. T., Terry, T. J. & Sakmar, T. P.
    Evidence that Helix 8 of rhodopsin acts as a membrane-dependent conformational switch.
    Biochemistry. 41:8298-8309 (2002).
  14. Sahu, S. K., Gummadi, S. N., Manoj, N., and Aradhyam, G. K.
    Phospholipid scramblases: an overview. Arch.
    Biochem. Biophys. 462(1):103-14 (2007).
  15. Padma Sree, T. N., Krishna Kumar, S., Senthilkumar, S., Aradhyam, G. K. and Sathyanarayana N.Gumadi, In vitro Effect of Terminalia arjuna Bark      Extract on Antioxidant Enzyme Catalase.” Journal of Pharmacology and Toxicology 2 (8): 698-708 (2007).
  16. Kamesh, N., Aradhyam, G. K., and Manoj, N.
    The repertoire of G protein-coupled receptors in the sea squirt Ciona intestinalis.
    BMC Evol. Biol. 8:129 (2008).
  17. Sahu, S. K., Gopala Krishna, A., and Gummadi, S. N.
    Over-expression of recombinant human phospholipid scramblase 1 in E. coli and its purification from inclusion bodies.
    Biotechnol. Lett. 30(12):2131-7(2008).
  18. Sahu, S. K., Aradhyam, G. K., and Gummadi, S. N.
    Calcium binding studies of peptides of human phospholipid scramblases 1 to 4 suggest that scramblases are new class of calcium binding proteins in the cell.
    Biochim. Biophys. Acta. 1790(10):1274-81(2009).
  19. Kanuru, M., Samuel, J. J., Balivada, L. M., and Aradhyam, G. K.
    Ion-binding properties of Calnuc, Ca2+ versus Mg2+–Calnuc adopts additional and unusual Ca2+-binding sites upon interaction with G-protein.
    FEBS J. 276(9):2529-46 (2009).
  20. Aradhyam, G. K., Balivada, L. M., Kanuru, M., Vadivel, P., and Vidhya, B. S. Calnuc: Emerging roles in calcium signaling and human diseases.
    UBMB Life. 62(6):436-46(2010).