Gautam Basu

Gautam Basu
Professor (retired), Biophysics

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Previous appointments:

1993-1995           Postdoctoral Fellow, Kyoto University

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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    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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