Publications

Please note: The copyrights to these publications are held by their publishers. The pdf files provided here may be used only for single copies for personal use, as though they were reprints provided by mail. They may not be reposted on other web sites or used for any other purpose without the permission of the appropriate publishers 

1. Bysack, A., Jash, C., and Raghuraman, H. (2025) Anionic lipids modulate the membrane localization and conformational dynamics of KirBac1.1 slide helix during lipid-dependent activation. Biochem. J. 482:1393-1413.  PDF

2. Bysack, A., Jash, C., and Raghuraman, H. (2025) Structural Dynamics of the Slide Helix of Inactive/Closed Conformation of KirBac1.1 in Micelles and Membranes: A Fluorescence Approach. J. Membr. Biol. 258:97-112.  PDF

3. Brahma, R., and Raghuraman, H. (2024) Characterization of a novel MgtE homolog and its structural dynamics in membrane mimetics. Biophys. J. 123 :1968-1983. PDF

4. Das, A., Bysack, A., and Raghuraman, H. (2024) Cholesterol modulates the structural dynamics of the paddle motif loop of KvAP voltage sensor. Curr. Res. Struct. Biol. 7:100137. PDF

5. Brahma, R., and Raghuraman, H. (2022) Measuring Membrane Penetration Depths and Conformational Changes in Membrane Peptides and Proteins. J. Membr. Biol. 255: 469-483. PDF

6. Brahma, R., and Raghuraman, H. (2022) Cost-effective Purification of Membrane Proteins using a Dual-detergent Strategy. Curr Protoc. 2 :e452. PDF

7. Brahma, R., Das, A., and Raghuraman, H. (2022) Site-directed fluorescence approaches to monitor the structural dynamics of proteins using intrinsic Trp and labeled with extrinsic fluorophores. STAR Protoc. 3: 101200. PDF

8. 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. 578: 122-128. PDF 

9. 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. PDF 

10. 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. PDF

11. 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. PDF

12. 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. PDF

13. 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 - Biophys. J. (2020) 118: 781-782 PDF ] PDF

14. 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. PDF

15. 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. PDF

16. 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. PDF

17. 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. PDF

18. 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. PDF

19. 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. PDF

20. 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. PDF

21. 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. PDF

22. 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. PDF

23. 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. PDF

24. 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. PDF

25. 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. PDF

26. Raghuraman, H., and Chattopadhyay, A. (2007) Orientation and dynamics of melittin in membranes of varying composition utilizing NBD fluorescence. Biophys. J. 92: 1271-1283. PDF

27. 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. PDF

28. Raghuraman, H., and Chattopadhyay, A. (2007) Melittin: A membrane-active peptide with diverse functions. Biosci. Rep. 27: 189-223. PDF

29. Mukherjee, S., Raghuraman, H., and Chattopadhyay, A. (2007) Membrane localization and dynamics of nile red: effect of cholesterol. Biochim. Biophys. Acta 1768: 59-66. PDF

30. 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. PDF

31. 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. PDF

32. 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. PDF

33. Raghuraman, H., and Chattopadhyay, A. (2005) Cholesterol inhibits the lytic activity of melittin in erythrocytes. Chem. Phys. Lipids 134: 183-189. PDF

34. Raghuraman, H., and Chattopadhyay, A. (2004) Interaction of melittin with membrane cholesterol: a fluorescence approach. Biophys. J. 87: 2419-2432. PDF

35. Raghuraman, H., and Chattopadhyay, A. (2004). Influence of lipid chain unsaturation on membrane-bound melittin: a fluorescence approach. Biochim. Biophys. Acta 1665: 29-39. PDF

36. 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. PDF

37. Raghuraman, H., and Chattopadhyay, A. (2004) Effect of micellar surface charge on the conformation and dynamics of melittin. Eur. Biophys. J. 33: 611-622. PDF

38. Chattopadhyay, A., and Raghuraman, H. (2004) Application of fluorescence spectroscopy to membrane protein structure and dynamics. Curr. Sci. 87: 175-180. PDF

39. 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. PDF

40. 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. PDF

41. Raghuraman, H., and Chattopadhyay, A. (2003) Organization and dynamics of melittin in environments of graded hydration: a fluorescence approach. Langmuir 19: 10332-10341. PDF

42. 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. PDF

43. 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.

44. 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. PDF