Research Highlight:

He is generally acknowledged as the father of modern scientific research in India.

Publications:

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-πinteractions: 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 suppressorprotein 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 humanLa 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 ofFluorescent Proteins: Spatially Enforced Communication of GFP andmCherry Encapsulated Within the P22 Capsid. Biomacromolecules 13:3902-3907.
17. Das, M., Basu, G.(2012)Glycine Rescue of β-Sheets fromcis-Proline. J. Am. Chem. Soc.134:13536-13539.
18. Das, L., Bhattacharya, B., Basu, G.(2012)Rationalization of paclitaxel insensitivity ofyeast β-tubulin and human βIII-tubulin isotype usingprincipal component analysis. BMC Research Notes5:395.
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-tRNAsynthetase also stabilizes a molten globule state. Biochemistry 51:4429-4437.
20. Dasgupta, S., Manna, D.,Basu, G. (2012)Structural and functional consequences ofmutating aproteobacteria-specific surface residue in thecatalytic domain of E. coli GluRS. FEBS Lett.586:1724-1730.
21. Ganguly, H. K., Majumder, B.,Chattopadhyay, S., Chakrabarti, P., Basu, G. (2012)DirectEvidence for CH-π Interaction Mediated Stabilization of Pro-cisProBond 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 MediatedDissociation of Mutagenic Ethidium from Synthetic DNA and VariousCell Nuclei. J. Phys. Chem. B115:14776-83.
23. Banerjee, S., Verma, P. K., Mitra, R. K.,Basu, G., Pal, S. K. (2011)Probing the Interior ofSelf-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 uniquebinding 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 transmembraneproteins.  Ind. J. Biochem. Biophys.48:106-110.  MAPSWebserver
26. Pradhan, S. K., Dasgupta, D., Basu G.(2011)Human telomere d[(TTAGGG)₄] undergoes aconformational transition to theNa+-form upon binding withsanguinarine 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 precursorfree synthesis and characterisation of stable Au nanochains by laserablation.  arXiv:1010.1999v1[cond-mat.mtrl-sci] .
28. Dasgupta, S., Saha, R.,Dey, C., Banerjee, R., Roy S, Basu G. (2009)The role of thecatalytic domain of E. coli GluRS in tRNAGln discrimination.  FEBS Lett. 583:2114-2120.
29. Banerjee R,Chattopadhyay S, Basu G. (2009)Conformational preferencesof ashort Aib/Ala-based water-soluble peptide as a functionoftemperature,  Proteins 76:184-200.
30. Das M, Basu G.(2009)Coulomb energies of protein-proteincomplexeswithmonopole-free charge distributions.J. Mol. Graph.Model. 27:846-51.
31. Saha R, Dasgupta S, BasuG, Roy S. (2009)A chimaeric glutamyl:glutaminyl-tRNAsynthetase: implications for evolution.Biochem. J. 417:449-55.
32. Dasgupta, B, Chakrabarti, P, Basu, G.(2007)Enhanced stability of cis Pro-Pro peptide bond inPro-Pro-Phesequence motif.FEBS Lett. 581:4529-32.
33. Banerjee M, Bhattacharyya, B., Basu, G. (2007)Differential colchicine-binding across eukaryoticfamilies: therole of highly conserved Pro268β and Ala248βresidues in animal tubulin.FEBS Lett. 581:5019-23.
34. Saha. R. P., Basu, G., Chakrabarti P.(2006)Cloning, expression, purification, and characterizationofVibrio cholerae transcriptional activator. HlyU.ProteinExpr. Purif. 48:118-25.
35. Allen M, Bulte JW,LiepoldL, Basu G, Zywicke HA, Frank JA, Young M, Douglas T.(2005)Paramagnetic viral nanoparticles as potentialhigh-relaxivity magnetic resonance contrast agents.Magn.Reson. Med. 54:807-812.
36. Gupta S, Banerjee M,PoddarA, Banerjee A, Basu G, Roy D, Bhattacharyya B.(2005)Biphasic kinetics of the colchicine-tubulininteraction:role of amino acids surrounding the a ring of boundcolchicine molecule.  Biochemistry 44:10181-10188.
37. Basu, G., Sivanesan,D., Kawabata, T., Go, N. (2004)Electrostatic Potential ofNucleotide-free Protein is Sufficient for DiscriminationBetweenAdenine and Guanine-specific Binding Sites.  J. Mol.Biol. 342:1053-1066.
38. Dasgupta, B., Pal,L.,Basu, G. & Chakrabarti, P. (2004)Expanded turnconformations: Characterization and sequence-structurecorrespondence in α-turns with implications in helixfolding.  Proteins 55:305-315.
39. Basu, G., Allen, M.,Willits, D., Young, M. & Douglas, T. (2003)Metal Bindingto Cowpea Mottle Virus Using Tb(III) Fluorescence.  J.Biol. Inorg. Chem. 8:721-725.
40. Pal,L., Chakrabarti, Basu, G. (2003)Sequence and StructuralPatterns in Proteins from an Analysisof 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 Predictionof 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 asanAla-based Peptide-Helix Double its Length.  ChemBioChem 3:1263-1266.
43. Banerjee, R., Basu, G.(2002)Direct evidence for alteration of unfolding profileofa helical peptide by far-ultraviolet circular dichroismaromaticside-chaincontribution.  FEBS Lett. 523:152-156..
44. Banerjee, R., Basu,G., Chene, P., Roy, S. (2002)Aib-based Peptide Backbone asScaffolds for Helical Peptide Mimics. J. Pep. Res. 60:88-94.
45. Pal, L., Basu, G.,Chakrabarti, P. (2002)Variants of 3₁₀-helices inProteins. 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 ofPhosphorylation on the Structure and Fold of Transactivationdomainof 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 Relaxationin 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 ofα-tubulin tail peptide: Implications for tail-bodyinteraction.Biochemistry 40:1512-15519.
50. Sengupta, J., Ray, P.K. & Basu, G. (2001)Solution structure of an immunoactivepeptide from Staphylococcal Protein A. J. Biomol. Struct.Dyn. 18:773-881.
51. Pal,L. & Basu, G. (2001)Neural Network Prediction of3₁₀-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) triadformation:designing novel structural elements into an existing DNAframework.J. Mol. Biol. 301:129-146.
53. Pal, L. & Basu, G.(1999)Novel protein structural motifs containing two-turn andlonger3₁₀-helices.Protein Eng. 12:811-814.
54. Basu, G., Kitao,A.,Kuki, A., & Go, N. (1998)Protein Electron TransferReorganization 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 ElectronTransfer Reorganization Energy Spectrum from Normal ModeAnalysis.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, inModular Chemistry ,J. Michl (ed.) pp 503 - 516Kluwer,Academic Publishers.
57. Chong, S., Miura, S.,Basu, G., & Hirata, F. (1995)A Molecular Theory for theNon-Equilibrium Free Energy Surface in Electron TransferReaction.J. Phys. Chem. 99:10526-10529.
58. Basu, G., Kitao, A.,Hirata, F., Go, N. (1994)A Collective Motion Description ofthe 3₁₀-/α-Helix Transition: Implications For aNatural Reaction Coordinate.J. Am. Chem. Soc.116:6307-6315.
59. Basu,G., Kubasik, M.,Anglos, D. & Kuki, A. (1993)Spin-Forbidden ExcitationTransfer and Heavy Atom Induced Intersystem Crossingin Linear andCyclic Peptides.J. Phys. Chem.97:3956-3967.
60. Basu, G., Anglos, D.,Kuki, A. (1993)Fluorescence Quenching in a Strongly HelicalPeptide Series: The Role of Non-Covalent Pathways in ModulatingElectronic Interaction.Biochemistry32:3067-3076.
61. Basu, G., Kuki, A.(1993)Evidence for a 3₁₀- helical Conformationofan Eight-Residue Peptide from 1H-1H Rotating Frame OverhauserStudies.Biopolymers 33:995-1000.
62. Basu, G., Kuki, A.(1992)Conformational Preferences of Oligopeptides Rich inα-Aminoisobutyric Acid. II. A Model For The 3₁₀- /α-Helical Transition with Composition and SequenceSensitivity.Biopolymers 32:61-71.
63. Basu, G., Bagchi, K.,Kuki, A. (1991)Conformational Preferences of OligopeptidesRich in α-aminoisobutyric Acid. I. Observation of a3₁₀- / α-HelicalTransition upon SequencePermutation.  Biopolymers31:1763-1774.
64. Basu, G.,Kubasik,M., Anglos, D., Secor, B. & Kuki, A. (1990)Long-RangeElectronic Interactions in Peptides: The Remote Heavy Atom Effect. J. Am. Chem. Soc. 112:9410-9411.

Awards/Recognition:

• Bose Institute was founded by Acharya Jagadish Chandra Bose, F.R.S., in 1917.
• The institute was one of the earliest, perhaps the first modern research institute in India.
• He is generally acknowledged as the father of modern scientific research in India.

Teaching:

• Bose Institute was founded by Acharya Jagadish Chandra Bose, F.R.S., in 1917.
• The institute was one of the earliest, perhaps the first modern research institute in India.
• He is generally acknowledged as the father of modern scientific research in India.

Present:

Previous:

Openings:

• Bose Institute was founded by Acharya Jagadish Chandra Bose, F.R.S., in 1917.
• The institute was one of the earliest, perhaps the first modern research institute in India.
• He is generally acknowledged as the father of modern scientific research in India.