Department of Atomic Energy, Govt. of India
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Prof. H. Raghuraman

Associate Professor
Room No : 309
Ext. : 1309
Email id : h.raghuraman[AT]
Division :
Structural dynamics of membrane proteins (ion channels and transporters), Lipid-protein interactions using Fluorescence and Electron Paramagnetic Resonance (EPR)-based approaches

  1. Das, A., Bysack, A., and Raghuraman, H. (2021) Effectiveness of dual-detergent strategy using Triton X-100 in membrane protein purification. Biochem. Biophys. Res. Commun. (in press).
  2. Das, A., and Raghuraman, H. (2021) Conformational heterogeneity of the voltage sensor loop of KvAP in micelles and membranes: a fluorescence approach. BBA-Biomembranes 1863: 183568.
  3. Brahma, R., and Raghuraman, H. (2021) Novel insights in linking solvent relaxation dynamics and protein conformations utilizing red edge excitation shift approach. Emerg. Top. Life Sci. 5: 89-101.
  4. Chatterjee, S., Brahma, R., and Raghuraman, H. (2021) Gating-related structural dynamics of the MgtE magnesium channel in membrane-mimetics utilizing site-directed tryptophan fluorescence. J. Mol. Biol. 433: 66691.
  5. Biswas, G., Ghosh, S., Raghuraman, H., and Banerjee, R. (2020) Probing conformational transitions of PIN1 from L. major during chemical and thermal denaturation. Int. J. Biol. Macromol. 154: 904-915.
  6. Das, A., Chatterjee, S., and Raghuraman, H. (2020) Structural dynamics of the paddle motif loop in the activated conformation of KvAP voltage sensor. Biophys. J. 118: 873-884. (New and Notable on this article)
  7. Raghuraman, H., Chatterjee, S., and Das, A. (2019) Site-directed fluorescence approaches for dynamic structural biology of membrane peptides and proteins. Front. Mol. Biosci. 6: 96.
  8. Chatterjee, S., Das, A., and Raghuraman, H. (2019) Biochemical and biophysical characterization of a prokaryotic Mg2+ ion channel: Implications for cost-effective purification of membrane proteins. Protein Expr. Purif. 161: 8-16.
  9. Kratochvil, H.T., Carr, J.K., Matulef, K., Annen, A.W., Li, H., Maj, M., Ostmeyer, J., Serrano, A.L., Raghuraman, H., Moran, S.D., Skinner, J.L., Perozo, E., Roux, B., Valiyaveetil, F.I., and Zanni, M.T. (2016) Instantaneous ion configurations in the K+ ion channel selectivity filter revealed by 2D IR spectroscopy. Science 353: 1040-1044.
  10. Pillai, V.B., Samant, S., Sundaresan, N.R., Raghuraman, H., Kim, G., Bonner, M.Y., Arbiser, J.L., Walker, D.I., Jones, D.P., Gius, D., and Gupta, M.P. (2015) Honokiol blocks and reverses cardiac hypertrophy in mice by activating mitochondrial Sirt3. Nat. Commun. 6: 6656.
  11. Raghuraman, H., Islam, S., Mukherjee, S., Roux, B., and Perozo, E. (2014) Dynamics transitions at the outer vestibule of the KcsA potassium channel during gating. Proc. Natl. Acad. Sci. USA 111: 1831-1836.
  12. White, E., Raghuraman, H*., Perozo, E., and Glotzer, M. (2013) Binding of CYK-4 subunit of the centralspindlin complex induces a large scale conformational change in the kinesin subunit. J. Biol. Chem. 288: 19785-19795.
  13. Raghuraman, H., Cordero-Morales, J., Jogini, V., Kollewe, A., and Perozo, E. (2012) Mechanism of Cd2+coordination during slow inactivation in potassium channels.  Structure 20: 1332-1342.
  14. Torbeev, V.Y., Raghuraman, H., Hamelberg, D., Tonelli, M., Westler, W.M., Perozo, E., Kent, S.B. (2011) Protein conformational dynamics in the mechanism of HIV-1 protease catalysis. Proc. Natl. Acad. Sci. USA 108: 20982-20987.
  15. Sundaresan, N.R., Pillai, V.B., Wolfgeher, D., Samant, S., Vasudevan, P., Parekh, V., Raghuraman, H., Cunningham, J.M., Gupta, M., and Gupta, M.P. (2011) The deacetylase SIRT1 promotes membrane localization and activation of Akt and PDK1 during tumorigenesis and cardiac hypertrophy. Sci. Signal. 4: ra46.
  16. Haldar, S., Raghuraman, H*., Namani, T., Rajarathnam, K., and Chattopadhyay, A. (2010) Membrane interaction of the N-terminal domain of chemokine receptor CXCR1. Biochim. Biophys. Acta 1798: 1056-1061.
  17. Torbeev, V.Y., Raghuraman, H., Mandal, K., Senapati, S., Perozo, E., and Kent, S.B.H. (2009) Dynamics of ‘Flap’ structures in three HIV-1 protease / inhibitor complexes probed by total chemical synthesis and pulse-EPR spectroscopy. J. Am. Chem. Soc. 131: 884-885.
  18. Haldar, S., Raghuraman, H., and Chattopadhyay, A. (2008) Monitoring orientation and dynamics of membrane-bound melittin utilizing dansyl fluorescence. J. Phys. Chem. B. 112: 14075-14082.
  19. Raghuraman, H., and Chattopadhyay, A. (2007) Orientation and dynamics of melittin in membranes of varying composition utilizing NBD fluorescence. Biophys. J. 92: 1271-1283.
  20. Raghuraman, H., Shrivastava, S., and Chattopadhyay, A. (2007) Monitoring the looping up of acyl chain labeled NBD lipids in membranes as a function of membrane phase state. Biochim. Biophys. Acta 1768: 1258-1267.
  21. Raghuraman, H., and Chattopadhyay, A. (2007) Melittin: A membrane-active peptide with diverse functions. Biosci. Rep. 27: 189-223.
  22. Mukherjee, S., Raghuraman, H., and Chattopadhyay, A. (2007) Membrane localization and dynamics of nile red: effect of cholesterol. Biochim. Biophys. Acta 1768: 59-66.
  23. Raghuraman, H., Ganguly, S., and Chattopadhyay, A. (2006) Effect of ionic strength on the organization and dynamics of membrane-bound melittin. Biophys. Chem. 124: 115-124.
  24. Raghuraman, H., and Chattopadhyay, A. (2006) Effect of ionic strength on folding and aggregation of the hemolytic peptide melittin in solution. Biopolymers 83: 111-121.
  25. Raghuraman, H., Kelkar, D.A., and Chattopadhyay, A. (2005) “Novel insights into protein structure and dynamics utilizing the red edge excitation shift approach” in Reviews in Fluorescence (Geddes, C.D., and Lakowicz, J.R., eds.), Springer, New York, pp. 199-214.
  26. Raghuraman, H., and Chattopadhyay, A. (2005) Cholesterol inhibits the lytic activity of melittin in erythrocytes. Chem. Phys. Lipids 134: 183-189.
  27. Raghuraman, H., and Chattopadhyay, A. (2004) Interaction of melittin with membrane cholesterol: a fluorescence approach. Biophys. J. 87: 2419-2432.
  28. Raghuraman, H., and Chattopadhyay, A. (2004). Influence of lipid chain unsaturation on membrane-bound melittin: a fluorescence approach. Biochim. Biophys. Acta 1665: 29-39.
  29. Raghuraman, H., Pradhan, S.K., and Chattopadhyay, A. (2004) Effect of urea on the organization and dynamics of Triton X-100 micelles: a fluorescence approach. J. Phys. Chem. B 108: 2489-2496.
  30. Raghuraman, H., and Chattopadhyay, A. (2004) Effect of micellar surface charge on the conformation and dynamics of melittin. Eur. Biophys. J. 33: 611-622.
  31. Chattopadhyay, A., and Raghuraman, H. (2004) Application of fluorescence spectroscopy to membrane protein structure and dynamics. Curr. Sci. 87: 175-180. 
  32. Mukherjee, S., Raghuraman, H., Dasgupta, S., and Chattopadhyay, A. (2004) Organization and dynamics of N-(7-nitrobenz-2-oxa-1,3,-diazol-4-yl)-labeled lipids: a fluorescence approach. Chem. Phys. Lipids 127: 91-101.
  33. Arora, A., Raghuraman, H., and Chattopadhyay, A. (2004) Influence of cholesterol and ergosterol on membrane dynamics: a fluorescence approach. Biochem. Biophys. Res. Commun. 318: 920-926.
  34. Raghuraman, H., and Chattopadhyay, A. (2003) Organization and dynamics of melittin in environments of graded hydration: a fluorescence approach. Langmuir 19: 10332-10341.
  35. Raghuraman, H., Kelkar, D.A., and Chattopadhyay, A. (2003) Novel insights into membrane protein structure and dynamics utilizing the wavelength-selective fluorescence approach. Proc. Ind. Natl. Sci. Acad. A 69: 25-35.
  36. Raghuraman, H., Mukherjee, S., and Chattopadhyay, A. (2002) "Organization and dynamics of micelles and reverse micelles utilizing wavelength-selective fluorescence approach" in IPS Newsletter (No. 41), pp. 61-65.
  37. Chattopadhyay, A., Mukherjee, S., and Raghuraman, H. (2002) Reverse micellar organization and dynamics: a wavelength-selective fluorescence approach. J. Phys. Chem. B. 106: 13002-13009. 
* equal contribution


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