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Research interests:

The focus of my research group is to understand biological problems at the molecular level where molecular structure plays a vital role. We use both experimental and theoretical / computational tools.


Address: Department of Biophysics
Centenary Campus
Bose Institute
P-1/12 C.I.T. Scheme VII-M
Kolkata - 700054, India
E-Mail: gautam[at]
Phone: +91-33-25693215



1.     Dasgupta, R., Ganguly, H. K., Modugula, E. K., Basu, G. (2016) Type VIa beta-turn-fused helix N-termini: A novel helix N-cap motif containing cis proline.   Biopolymers (Peptide Science) (DOI: 10.1002/bip.22919)

2.     Mahata, T., Kanungo, A., Ganguly, S., Modugula, E. K., Choudhury, S., Pal, S. K., Basu, G., Dutta, S. (2016) The Benzyl Moiety in a Quinoxaline-Based Scaffold Acts as a DNA Intercalation Switch.   Angew. Chem. Int. Ed. Engl. 55:7733-7736.

3.     Chattopadhyay, S., Haresh, A., Basu, G. (2016) Effect of introducing Aib in a designed helical inhibitor of HDM2-p53 interaction: A molecular dynamics study.   Biopolymers (Peptide Science) 106:51-61.

4.     Jordan, P. C., Patterson, D. P., Saboda, K. N., Edwards, E. J., Mietten-Granger, H., Basu, G., Thielges, M. C., Douglas, T. (2016) Self-Assembling Biomolecular Catalysts for Hydrogen Production.   Nature Chemistry 8:179-185.

5.     Schwarz, B., Madden, P., Avera, J., Gordon, B., Larson, K., Mietten, H., Uchida, M., LaFrance, B., Basu, G., Rynda-Apple, A., Douglas, T. (2015) Symmetry Controlled, Genetic Presentation of Bio-Active Proteins on the P22 Virus-like Particle using Bacteriophage L Decoration Protein.   ACS Nano 9:9134-9147.

6.     Das, M., Basu, G. (2015) Protein-protein association rates captured in a single geometric parameter.   Proteins: Structure, Function and Bioinformatics 83:1557-1562.

7.     Chongdar, N., Dasgupta, S., Dutta, A. B., Basu, G. (2015) Dispensability of zinc and the putative zinc-binding domain in bacterial glutamyl-tRNA synthetase.   Biosci. Rep. 35:e00184.

8.     Chongdar, N., Dasgupta, S., Dutta, A. B., Basu, G. (2014) Preliminary X-ray crystallographic analysis of an engineered glutamyl-tRNA synthetase from Escherichia coli   Acta Crystallogr. F Struct. Biol. Commun. 70:922-927.

9.     Dasgupta, S., Basu, G. (2014) Evolutionary insights about bacterial GlxRS from whole genome analyses: Is GluRS2 a chimera?   BMC Evol. Biol. 14:26.

10.   Kumar, A., Manna, A., Ray, U., Mullick, R., Basu, G., Das, S., Roy, S. (2014) Specific Sequence of a Beta-turn in Human La Protein May Contribute to Species Specificity of Hepatitis C Virus   J. Virol. 88:4319-4327. 

11.   Goswami, N., Baksi, A., Giri, A., Xavier, P.L., Basu, G., Pradeep, T., Pal, S.K. (2014) Luminescent iron clusters in solution.   Nanoscale 6:1848-1854. 

12.   Chakraborti, S., Dhar, G., Dwivedi, V., Das, A., Poddar, A., Chakrabarti, G., Basu, G., Chakrabarti, P., Surolia, A., Bhattacharyya, B. (2013) Stable and potent analogs derived from the modification of the dicarbonyl moiety of curcumin.   Biochemistry 52:7449-7460. 

13.   Ganguly, H. K., Kaur, H., Basu, G. (2013) Local control of cis-peptidyl-prolyl bonds mediated by CH-π interactions: The Xaa-Pro-Tyr motif.   Biochemistry 52:6348-6357. 

14.   Das, S., Banerjee, B., Hossain, M., Thangamuniyandi, M., Dasgupta, S., Chongdar, N., Suresh Kumar, G., Basu, G. (2013) Characterization of DNA binding property of the tumor suppressor protein Integrase Interactor 1 (INI1/hSNF5).   Plos One 8:e66581.

15.   Manna, A. K., Kumar A., Ray, U., Das, S., Basu, G., Roy, S. (2013) A cyclic peptide mimic of an RNA recognition motif of human La protein is a potent inhibitor of hepatitis C virus.   Antiviral Res. 97:223-226.

16.   O'Neil, A., Prevelige, P. E., Basu, G., Douglas, T. (2012) Co-Confinement of Fluorescent Proteins: Spatially Enforced Communication of GFP and mCherry Encapsulated Within the P22 Capsid.   Biomacromolecules 13:3902-3907.

17.   Das, M., Basu, G. (2012) Glycine Rescue of β-Sheets from cis-Proline.   J. Am. Chem. Soc. 134:13536-13539.

18.   Das, L., Bhattacharya, B., Basu, G. (2012) Rationalization of paclitaxel insensitivity of yeast β-tubulin and human βIII-tubulin isotype using principal component analysis.   BMC Research Notes 5:395.

19.   Saha, R., Dasgupta, S., Banerjee, R., Mitra-Bhattacharyya, A., Soll, D., Basu, G., Roy, S. (2012) A functional loop spanning distant domains of glutaminyl-tRNA synthetase also stabilizes a molten globule state.   Biochemistry 51:4429-4437.

20.   Dasgupta, S., Manna, D., Basu, G. (2012) Structural and functional consequences of mutating a proteobacteria-specific surface residue in the catalytic domain of E. coli GluRS.   FEBS Lett. 586:1724-1730.

21.   Ganguly, H. K., Majumder, B., Chattopadhyay, S., Chakrabarti, P., Basu, G. (2012) Direct Evidence for CH-π Interaction Mediated Stabilization of Pro-cisPro Bond in Peptides with Pro-Pro-Aromatic motifs.   J. Am. Chem. Soc. 134:4661-4669.

22.   Banerjee, S., Bhowmik, D., Verma, P. K., Mitra, R. K., Sidhhanta, A., Basu, G., Pal, S. (2011) Ultrafast Spectroscopic Study on Caffeine Mediated Dissociation of Mutagenic Ethidium from Synthetic DNA and Various Cell Nuclei.   J. Phys. Chem. B 115:14776-83.

23.   Banerjee, S., Verma, P. K., Mitra, R. K., Basu, G., Pal, S. K. (2011) Probing the Interior of Self-Assembled Caffeine Dimer at Various Temperatures.   J. Fluoresc. 22:753-69.

24.   Chakraborti, S., Das, L., Kapoor, N., Das, A., Dwivedi, V., Poddar, A., Chakrabarti, G., Janik, M. E., Basu, G., Panda, D., Chakrabarti, P., Surolia, A., Bhattacharyya, B. (2011) Curcumin recognizes a unique binding site of tubulin.   J. Med. Chem. 54:6183-6196.

25.   Cheema, J. and Basu G. (2011) MAPS: An interactive web server for membrane annotation of transmembrane proteins.   Ind. J. Biochem. Biophys. 48:106-110.  MAPS Webserver

26.   Pradhan, S. K., Dasgupta, D., Basu G. (2011) Human telomere d[(TTAGGG)4] undergoes a conformational transition to the Na+-form upon binding with sanguinarine in presence of K+.   Biochem. Biophys. Res. Comm. 404:139-142. 

27.   Neogy, R. K., Nath, R., Basu, G., Raychaudhuri, A. K. (2010) Single step precursor free synthesis and characterisation of stable Au nanochains by laser ablation.   arXiv:1010.1999v1 [cond-mat.mtrl-sci] .

28.   Dasgupta, S., Saha, R., Dey, C., Banerjee, R., Roy S, Basu G. (2009) The role of the catalytic domain of E. coli GluRS in tRNAGln discrimination.   FEBS Lett. 583:2114-2120.

29.   Banerjee R, Chattopadhyay S, Basu G. (2009) Conformational preferences of a short Aib/Ala-based water-soluble peptide as a function of temperature,  Proteins 76:184-200.

30.   Das M, Basu G. (2009) Coulomb energies of protein-protein complexes with monopole-free charge distributions. J. Mol. Graph. Model. 27:846-51.

31.   Saha R, Dasgupta S, Basu G, Roy S. (2009) A chimaeric glutamyl:glutaminyl-tRNA synthetase: implications for evolution. Biochem. J. 417:449-55. 

32.   Dasgupta, B, Chakrabarti, P, Basu, G. (2007) Enhanced stability of cis Pro-Pro peptide bond in Pro-Pro-Phe sequence motif. FEBS Lett. 581:4529-32. 

33.  Banerjee M, Bhattacharyya, B., Basu, G. (2007) Differential colchicine-binding across eukaryotic families: the role of highly conserved Pro268β and Ala248β residues in animal tubulin. FEBS Lett. 581:5019-23. 

34.   Saha. R. P., Basu, G., Chakrabarti P. (2006) Cloning, expression, purification, and characterization of Vibrio cholerae transcriptional activator. HlyU. Protein Expr. Purif. 48:118-25. 

35.  Allen M, Bulte JW, Liepold L, Basu G, Zywicke HA, Frank JA, Young M, Douglas T. (2005) Paramagnetic viral nanoparticles as potential high-relaxivity magnetic resonance contrast agents. Magn. Reson. Med. 54:807-812. 

36.  Gupta S, Banerjee M, Poddar A, Banerjee A, Basu G, Roy D, Bhattacharyya B. (2005) Biphasic kinetics of the colchicine-tubulin interaction: role of amino acids surrounding the a ring of bound colchicine molecule.   Biochemistry 44:10181-10188. 

37.  Basu, G., Sivanesan, D., Kawabata, T., Go, N. (2004) Electrostatic Potential of Nucleotide-free Protein is Sufficient for Discrimination Between Adenine and Guanine-specific Binding Sites.   J. Mol. Biol. 342:1053-1066. 

38.   Dasgupta, B., Pal, L., Basu, G. & Chakrabarti, P. (2004) Expanded turn conformations: Characterization and sequence-structure correspondence in α-turns with implications in helix folding.   Proteins 55:305-315.  

39.   Basu, G., Allen, M., Willits, D., Young, M. & Douglas, T. (2003) Metal Binding to Cowpea Mottle Virus Using Tb(III) Fluorescence.   J. Biol. Inorg. Chem. 8:721-725. 

40.   Pal, L., Chakrabarti, Basu, G. (2003) Sequence and Structural Patterns in Proteins from an Analysis of the Shortest Helices: Implications for helix nucleation.  J. Mol. Biol. 326:273-291. 

41.   Tanimoto, S., Basu, G., Kawabata, T., Go, N. (2003) On the Accuracy of Transmembrane Segment Prediction of Helical Integral Membrane Proteins.   Genome Informatics 14: 557-558. 

42.   Banerjee, R., Basu, G. (2002) A Short Aib/Ala-based Peptide-helix is as Stable as an Ala-based Peptide-Helix Double its Length.   ChemBioChem 3:1263-1266. 

43.   Banerjee, R., Basu, G. (2002) Direct evidence for alteration of unfolding profile of a helical peptide by far-ultraviolet circular dichroism aromaticside-chain contribution.  FEBS Lett. 523:152-156..

44.   Banerjee, R., Basu, G., Chene, P., Roy, S. (2002) Aib-based Peptide Backbone as Scaffolds for Helical Peptide Mimics. J. Pep. Res. 60:88-94. 

45.   Pal, L., Basu, G., Chakrabarti, P. (2002) Variants of 310-helices in Proteins. Proteins 48, 571:579.

46.   Kar, S., Sakaguchi, K., Shimohigashi, Y., Samaddar, S., Banerjee, R., Basu, G., Swaminathan, V., Kundu, T. K., Roy, S. (2002) Effect of Phosphorylation on the Structure and Fold of Transactivation domain of p53. J. Biol. Chem. 277:15579-15585.

47.   Sivanesan, D., Basu, G., Go, N. (2002) The Role of Electrostatics in Discrimination of Adenine and Guanine by Proteins.   Genome Informatics 13: 316-317. 

48.   Ghose, M., Mandal, S., Roy, D., R. K. Mandal, Basu, G. (2001) Dielectric Relaxation in a Single Tryptophan Protein. FEBS Lett. 509:337-340. 

49.   Pal, D., Mahapatra, P., Manna, T., Chakrabarti, P., Bhattacharyya, B., Banerjee, A., Basu, G., Roy, S. (2001) Conformational properties of α-tubulin tail peptide: Implications for tail-body interaction. Biochemistry 40:1512-15519.

50.   Sengupta, J., Ray, P. K. & Basu, G. (2001) Solution structure of an immunoactive peptide from Staphylococcal Protein A. J. Biomol. Struct. Dyn. 18:773-881.

51.   Pal, L. & Basu, G. (2001) Neural Network Prediction of 310-helices in proteins. Ind. J. Biochem. Biophys. 38:107-114.

52.   Kettani, A., Basu, G., Gorin, A., Majumdar, A., Skripkin, E. & Patel, D. J. (2000) A two-stranded template-based approach to G.(C-A) triad formation: designing novel structural elements into an existing DNA framework. J. Mol. Biol. 301:129-146. 

53.   Pal, L. & Basu, G. (1999) Novel protein structural motifs containing two-turn and longer 310-helices. Protein Eng. 12:811-814. 

54.   Basu, G., Kitao, A., Kuki, A., & Go, N. (1998) Protein Electron Transfer Reorganization Energy Spectrum from Normal Mode Analysis. II. Application to Ru-modified Cytochrome c. J. Phys. Chem. B 102:2085-2094. 

55.   Basu, G., Kitao, A., Kuki, A., & Go, N. (1998) Protein Electron Transfer Reorganization Energy Spectrum from Normal Mode Analysis. I. Theory. J. Phys. Chem. B 102:2076-2084. 

56.   Kuki, A., Anglos, A., Augspurger, J. D., Basu, G., Bindra, V. A., Kubasik, M., Pettijohn, A. (1997) Molecular Optical Rails Based on Aib, in Modular Chemistry , J. Michl (ed.) pp 503 - 516 Kluwer, Academic Publishers.

57.   Chong, S., Miura, S., Basu, G., & Hirata, F. (1995) A Molecular Theory for the Non-Equilibrium Free Energy Surface in Electron Transfer Reaction. J. Phys. Chem. 99:10526-10529. 

58.   Basu, G., Kitao, A., Hirata, F., Go, N. (1994) A Collective Motion Description of the 310-/α-Helix Transition: Implications For a Natural Reaction Coordinate. J. Am. Chem. Soc. 116:6307-6315. 

59.   Basu, G., Kubasik, M., Anglos, D. & Kuki, A. (1993) Spin-Forbidden Excitation Transfer and Heavy Atom Induced Intersystem Crossing in Linear and Cyclic Peptides. J. Phys. Chem. 97:3956-3967.

60.   Basu, G., Anglos, D., Kuki, A. (1993) Fluorescence Quenching in a Strongly Helical Peptide Series: The Role of Non-Covalent Pathways in Modulating Electronic Interaction. Biochemistry 32:3067-3076.

61.   Basu, G., Kuki, A. (1993) Evidence for a 310- helical Conformation of an Eight-Residue Peptide from 1H-1H Rotating Frame Overhauser Studies. Biopolymers 33:995-1000.

62.   Basu, G., Kuki, A. (1992) Conformational Preferences of Oligopeptides Rich in α-Aminoisobutyric Acid. II. A Model For The 310- / α-Helical Transition with Composition and Sequence Sensitivity. Biopolymers 32:61-71. 

63.   Basu, G., Bagchi, K., Kuki, A. (1991) Conformational Preferences of Oligopeptides Rich in α-aminoisobutyric Acid. I. Observation of a 310- / α-Helical Transition upon Sequence Permutation.   Biopolymers 31:1763-1774. 

64. Basu, G., Kubasik, M., Anglos, D., Secor, B. & Kuki, A. (1990) Long-Range Electronic Interactions in Peptides: The Remote Heavy Atom Effect. J. Am. Chem. Soc. 112:9410-9411.

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    Integrated MSc-PhD:


    Image Name Designation Department Campus Contact number Email
    profile image Chandradeep Basu Junior Research Fellow Biophysics Centenary 25693215
    profile image Sudakshina Ganguly Senior Research Fellow Biophysics Centenary 25693218 sudakshina


    Group Members:

    Dr. Aditya Dev (Research Associate)
    Dr. Debamitra Chakravorty(Research Associate)
    Bankim Mandal (Senior Research Fellow)
    Sudakshina Ganguly (Senior Research Fellow)
    Chandradeep Basu (Junior Research Fellow)

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