PhD: Indian Institute of Science, Bangalore, 1981
Swiss Federal Institute of Technology, Zürich (with Prof. J. D. Dunitz, FRS, 1981-1982).
Purdue University, West Lafayette, USA (with Prof. M. G. Rossmann, 1982-1984).
University of California, Los Angeles (with Prof. D. C. Rees, 1984-1989)
Research Fellow, California Institute of Technology (with 1989-1990).
Scientist, National Chemical Laboratory, Pune (1990-1997).
Associate Professor, Professor, Senior Professor, Bose Institute (1997-present)
Understanding the structure and folding of proteins and their interactions with other molecules, large and small, and nanoparticles using biophysical techniques (especially, X-ray crystallography), modelling and database analysis. Some specific topics are:
- Identification of stabilizing interactions (like CH-p, CH-O, electrophile-nucleophile, aromatic-aromatic etc.) and their implications in protein structures and function
- Analysis of protein conformation and identification of structural motifs
- Protein folding, threading and prediction of structures
- Molecular modelling and dynamics to understand protein function
- Molecular recognition, protein-protein/DNA complexation and ion-binding by proteins
- Biophysical studies on proteins from phage lambda and Vibrio cholerae
- Design of peptides with specific structure
- Structural bioinformatics and development of algorithms
- Vibrio cholerae proteomics
- Interaction of nanoparticles with proteins and their antibacterial effect.
Department of Biochemistry
P-1/12 C.I.T. Scheme VII-M
Kolkata - 700054, India
The work encompasses structural biology,
proteomics and bioinformatics. Both experimental and theoretical techniques are
used for getting insight into aspects of protein structure, function and
1) Nobel Laureate Linus Pauling had proposed important protein secondary structures, a-helix and b-sheet. From an exhaustive analysis of protein structures we have discovered a new secondary structure, which because of its shape is termed topi (hat in many Indian languages). Thus we have introduced an Indian term in scientific lexicon (Dhar J, Kishore R and Chakrabarti P. Scientific Reports, 6:31483 (2016).
2) Following the tradition of GN Ramachandran we have done extensive work on protein structure, conformation and weak interactions that stabilize the native fold. A review article with authors from three other countries on C-H···p interactions (Nishio M, Umezawa Y, Fantini J, Weiss MS and Chakrabarti P. Phys. Chem. Chem. Phys. 16, 12648 (2014)) has been highly acclaimed.
3) We have been involved in understanding the process of molecular recognition by analyzing the physicochemical and evolutionary properties of interfaces formed in protein-protein/DNA complexes. Our dissection of the interface into core and rim (Chakrabarti P and Janin J. Proteins, 47, 334 (2002)) is now referred to as CJ model (Levy E. J Mol Biol 403, 660 (2010)). This is one of the most highly cited papers from the institute (~600 citations). The residues in the core are more conserved than those in rim, which has led to the development of an algorithm of for predicting the hotspot residues in interfaces (Guharoy M and Chakrabarti P. Proc. Natl. Acad. Sci. USA, 102, 15447 (2005)).
4) Many of the webservers (on protein-protein interaction) developed in the lab (http://www.boseinst.ernet.in/resources/bioinfo/stag.html) are being widely used (Saha RP, Bahadur R, Pal A, Mandal S and Chakrabarti P. BMC Struct. Biol. 6, 11 (2006)).
5) We are involved in crystallographic analysis of a number of interesting proteins, such as CII from bacteriophage lambda, which is the deciding factor in which of the two alternative modes (lysis or lysogeny) bacteriophage lambda develops. The structure explains why this transcription activator binds a direct repeat DNA sequence (Datta AB, Panjikar S, Weiss MS, Chakrabarti P and Parrack P. Proc. Natl. Acad. Sci. USA, 102, 11242 (2005)).
6) Another topic of interest is the structural proteomics of Vibrio chholerae. Structures have been elucidated for HlyU (transcriptional activator of the hemolysin gene hlyA) (Mukherjee D, Datta AB and Chakrabarti P. Biochim. Biophys. Acta 1844, 2346-2354 (2014)) and PIMT (a repair enzyme) (Chatterjee T et al. Arch. Biochem. Biophys. 583, 140 (2015)). EMSA has been used to delineate the DNA binding sequence (173 bp upstream of hlyA promoter), and mutational studies carried out to identify the residues in the recognition helix and the wing region of HlyU involved in the interaction (Mukherjee D, Pal A, Chakravarty D and Chakrabarti P. Nucleic Acids Res. 43, 1407-1417 (2015)). The effect of virstatin on the DNA binding property of ToxR, a transcriptional activator of two major virulence factors for cholera pathogenesis, cholera toxin (CT) and toxin coregulated pilus (TCP), has been elucidated.
7) Our work involving the antimicrobial and anti-tumor activity of ZnO nanoparticles and their surface-coated derivatives is likely to find niche applications in pharmaceutical industry (Sarwar S, Chakraborti S, Bera S, Sheikh IA, Hoque KM and Chakrabarti P. Nanomedicine, 12, 1499-1509 (2016)). The effect of morphology and size of gold nanoparticles on the growth of V. cholerae biotypes and accessory cholera enterotoxin (Ace) have been studied using biophysical methods and animal studies (Chatterjee T, Chatterjee B, Saha T, Hoque KM and Chakrabarti P. Biochem Biophys Acta, 1861, 977 (2017)). The bacterial growth kinetics has been modeled to incorporate the antibacterial effect of silver nanoparticles (Chatterjee T, Chatterjee BK, Majumdar D and Chakrabarti P. Biochim. Biophys. Acta, 1850, 299 (2015)).
8) Biophysical techniques and MD simulations have been used to understand
the binding of small molecules to proteins and the dynamics of binding (Chakraborti
S, Dhar G, Dwivedi V, Das A, Poddar A, Chakraborti G, Basu G, Chakrabarti P,
Surolia A and Bhattacharyya B. Biochemistry 52, 7449 (2013)). In silico mutations and molecular
dynamics have been used to understand the importance of flexibility in the
N-terminal actin-binding domain (Chakravarty D, Chakraborti S and Chakrabarti P.
Proteins, 83, 696 (2015)).
1. Maji A, Beg M, Mandal AM, Das S, Jha PK, Kumar A, Sarwar S, Hossain M and Chakrabarti P (2017). Spectroscopic interaction study of human serum albumin and human haemoglobin with Mersilea quadrifolia leaves extract mediated silver nanoparticles having antibacterial and anticancer activity. J Mol Struct, 1141, 584-592.
2. Jana TK, Pal A, Mandal AK, Sarwar S, Chakrabarti P and Chatterjee K (2017). Photocatalytic and antibacterial performance of a-Fe2O3 nanostructures. Chemistry Select (in press. Doi: 10.1002/slct.201700294).
3. Chatterjee T, Chatterjee B, Saha T, Hoque KM and Chakrabarti P (2017). Structure and function of Vibrio cholerae accessory cholera enterotoxin in presence of gold nanoparticles: Dependence on morphology. Biochim. Biophys. Acta, 1861, 977-986.
4. Chakraborti S, Chakraborty S, Saha S, Manna A, Banerjee S, Adhikary A, Sarwar S, Hazra TK, Das T and Chakrabarti P (2017). PEG-functionalized zinc oxide nanoparticles induce apoptosis in breast cancer cells through reactive oxygen species-dependent impairment of DNA damage repair enzyme NEIL2. Free Radical Biology & Medicine, 103, 35-47.
5. Aoun J, Hayashi M, Sheikh IA, Sarkar P, Saha T, Ghosh P, Bhowmick R, Ghosh D, Chatterjee T, Chakrabarti P, Chakrabarti MK, Hoque KM (2016). Anoctamin 6 contributes to Cl- secretion in accessory cholera enterotoxin (Ace) stimulated diarrhea: an essential role for PIP2 signaling in cholera. J Biol Chem, 291, 26816-26836.
6. Dhar J, Kishore R and Chakrabarti P (2016). A novel secondary structure based on fused five-membered rings motif. Scientific Reports, 6:31483.
7. Ghosh T, Barik S, Bhuniya A, Dhar J, Dasgupta S, Ghosh S, Sarkar M, Guha I, Sarkar K, Chakrabarti P, Saha B, Storkus WJ, Baral R and Bose A (2016). Tumor-associated mesenchymal stem cells inhibit naïve T cell expansion by blocking cysteine export from dendritic cells. Int J Cancer, 139, 2068-2081.
8. Karaman DS, Sarwar S, Desai D, Björk EM, Odén M, Chakrabarti P, Rosenholm JM and Chakraborti S (2016). Shape engineering boosts antibacterial activity of chitosan coated mesoporous silica nanoparticle doped with silver: a mechanistic investigation. J. Mater. Chem. B, 4, 3292-3304.
9. Sarwar S, Chakraborti S, Bera S, Sheikh IA, Hoque KM and Chakrabarti P (2016). The antimicrobial activity of ZnO nanoparticles against Vibrio cholerae: Variation in response depends on biotype. Nanomedicine, 12, 1499-1509.
10. Biswas S and Chakrabarti P (2016). Analysis of interactions and dissection of interfaces involved in RNA-protein recognition. Protein & Peptide Letters, 23, 777-784.
11. Chatterjee T, Sheikh IA, Chakravarty D, Chakrabarti P, Sarkar P, Saha T, Chakrabarti MK and Hoque KM (2015). Effects of small molecule calcuium-activated chloride channel inhibitors on structure and function of Accessory cholera enterotoxin (Ace) of Vibrio cholerae. PLoS ONE, 10(11): e0141283.
12. Chakravarty D, Janin J, Robert CH and Chakrabarti P (2015). Changes in protein structure at the interface accompanying complex formation. IUCr J, 2, 643-652. (Scientific Commentary on the article: Laskowski RA and Thornton JM. ibid, 609-610).
13. Chatterjee T, Mukherjee D, Banerjee M, Chatterjee BK and Chakrabarti P (2015). Crystal structure and activity of protein L-isoaspartyl-O-methyltransferase from Vibrio cholerae, and the effect of AdoHcy binding. Arch. Biochem. Biophys. 583, 140-149.
14. Dhar J and Chakrabarti P (2015). Defining the loop structures in proteins based on composite b-turn mimics. Protein Engng, Design & Selection, 28, 153-161.
15. Chakravarty D, Chakraborti S and Chakrabarti P (2015). Flexibility in the N-terminal actin-binding domain: Clues from in sillico mutations and molecular dynamics. Proteins, 83, 696-710.
16. Dhar G, Chakravarty D, Hazra J, Dhar J, Poddar A, Pal M, Chakrabarti P, Surolia A and Bhattacharyya B (2015). Actin-curcumin interaction: Insights into the mechanism of actin polymerization inhibition. Biochemistry, 54, 1132-1143.
17. Mukherjee D, Pal A, Chakravarty D and Chakrabarti P (2015). Identification of the target DNA sequence and characterization of DNA binding features of HlyU, and suggestion of a redox switch for hlyA expression in the human pathogen Vibrio cholerae from in silico studies. Nucleic Acids Res. 43, 1407-1417.
18. Chatterjee T, Chatterjee BK, Majumdar D and Chakrabarti P. Antibacterial effect of silver nanoparticles and the modeling of bacterial growth kinetics using a modified Gompertz model (2015). Biochim. Biophys. Acta, 1850, 299-306.
19. Dhar J, Chakrabarti P, Saini H, Raghava GPS, Kishore R (2015). w-Turn: a novel b-turn mimic in globular proteins stabilized by main-chain to side-chain C-H×××O interaction. Proteins, 83, 203-214.
20. Mukherjee D, Datta AB and Chakrabarti P (2014). Crystal structure of HlyU, the hemolysin gene transcription activator, from Vibrio cholerae N16961 and functional implications. Biochim. Biophys. Acta 1844, 2346-2354.
21. Chakraborti S, Mandal AK, Sarwar S, Singh P, Chakraborty R and Chakrabarti P (2014). Bactericidal effect of polyethyleneimine capped ZnO nanoparticles on multiple antibiotic resistant bacteria harboring genes of high-pathogenicity island. Colloids and Surfaces B: Biointerfaces, 121, 44-53.
22. Nishio M, Umezawa Y, Fantini J, Weiss MS, and Chakrabarti P (2014). CH/p hydrogen bonds in biological macromolecules. Phys. Chem. Chem. Phys. 16, 12648-12683.
23. Dasgupta B, Dey S and Chakrabarti P (2014). Water and side-chain embedded p-turns. Biopolymers, 101, 441-453.
24. Chakraborti S, Dhar G, Dwivedi V, Das A, Poddar A, Chakraborti G, Basu G, Chakrabarti P, Surolia A and Bhattacharyya B (2013). Stable and potent analogues derived from the modification of the dicarbonyl moiety of curcumin. Biochemistry 52, 7449-7460.
25. Chakraborti S, Sarwar S and Chakrabarti P (2013). The effect of the binding of ZnO nanoparticle on the structure and stability of a-lactalbumin: a comparative study. J. Phys. Chem. B 117, 13397-13408.
26. Chakravarty D, Guharoy M, Robert CH, Chakrabarti P and Janin J (2013). Reassessing buried surface areas in protein-protein complexes. Protein Sci. 22, 1453-1457.
27. Chakraborti S, Bhattacharya S, Chowdhury R and Chakrabarti P (2013). The molecular basis of inactivation of metronidazole-resistant Helicobacter pylori using polyethyleneimine functionalized zinc oxide nanoparticles. PLoS ONE, 8(8): e70776.
28. Chatterjee T, Pal A, Chakravarty D, Dey S, Saha RP and Chakrabarti P (2013). Protein L-isoaspartyl-O-methyltransferase of Vibrio cholerae: Interaction with cofactors and effect of osmolytes on unfolding. Biochimie, 95, 912-921.
29. Chakraborti S, Chakravarty D, Gupta S, Chatterje, BP, Dhar G, Poddar A, Panda D, Chakrabarti P, Dastidar SG, Bhattacharyya B (2012). Discrimination of ligands with different flexibilities resulting from the plasticity of the binding site in tubulin. Biochemistry, 51, 7138-7148.
30. Chakraborti S, Joshi P, Chakravarty D, Shanker V, Ansari ZA, Singh SP and Chakrabarti P (2012). Interaction of polyethyleneimine functionalized ZnO nanoparticles with bovine serum albumin. Langmuir, 28, 11142-11152.
31. Dey S, Pal A, Guharoy M, Sonavane S and Chakrabarti P (2012). Characterization and prediction of the binding site in DNA-binding proteins: improvement of accuracy by combining residue composition, evolutionary conservation and structural parameters. Nucleic Acids Res. 40, 7150-7161.
32. Chatterjee T, Pal A, Dey S, Chatterjee BK and Chakrabarti P (2012). Interaction of virstatin with human serum albumin: spectroscopic analysis and molecular modeling. PLoS ONE, 7(5): e37468.
33. Joshi P, Chakraborti S, Chakrabarti P, Sing SP, Ansari ZA, Husain M and Shanker V (2012). ZnO nanoparticles as an antibacterial agent against E.coli. Sci. Adv. Mater. 4(1), 173-178.
34. Joshi P, Chakraborti S, Ramirez-Vick JE, Ansari ZA, Shanker V, Chakrabarti P and Singh SP (2012). The anticancer activity of chloroquine-gold nanoparticles against MCF-7 breast cancer cells. Colloids Surfaces B: Biointerfaces, 95, 195-200.
35. Mazumder A, Bandyopadhyay S, Dhar A, Lewis DEA, Deb S, Dey S, Chakrabarti P and Roy S (2012). A genetic network that balances two outcomes utilizes asymmetric recognition of operator sites. Biophys. J. 102, 1580-1589.
36. Ganguly HK, Majumder B, Chattopadhyay S, Chakrabarti P and Basu G (2012). Direct evidence for CH···p interaction mediated stabilization of Pro-cisPro bond in peptides with Pro-Pro-Aromatic motifs. J. Amer. Chem. Soc. 134, 4661-4669.
37. Dey S, Chakrabarti P and Janin J (2011). A survey of hemoglobin quaternary structures. Proteins, 79, 2861-2870.
38. Chakraborti S, Das L, Kapoor N, Das A, Dwivedi V, Poddar A, Chakraborti G, Janik M, Basu G, Panda D, Chakrabarti P, Surolia A and Bhattacharyya B (2011). Curcumin recognizes a unique binding site of tubulin. J. Med. Chem. 54, 6183-6196.
39. Kumar A, Chakraborti S, Joshi P, Chakrabarti P and Chakraborty R (2011). A multiple antibiotic and serum resistant oligotrophic strain, Klebsiella pneumoniae MB45 having novel dfrA30, is sensitive to ZnO QDs. Ann Clin Microbiol Antimicrob 10:19.
40. Chakraborty S, Joshi P, Shanker V, Ansari ZA, Singh SP and Chakrabarti P (2011). Contrasting effect of gold nanoparticles and nanorods on the structure and activity of bovine serum albumin. Langmuir, 27, 7722-7731.
41. Chatterjee T, Mukherjee D, Dey S, Pal A, Hoque KM and Chakrabarti P (2011). Accessory cholera enterotoxin, Ace, from Vibrio cholerae: Structure, unfolding, and virstatin binding. Biochemistry 50, 2962-2972.
42. Guharoy M, Pal A, Dasgupta M and Chakrabarti P (2011). PRICE (PRotein Interface Conservation and Energetics): a server for the analysis of protein-protein interfaces. J. Struct. Func. Genom. 12, 33-41.
43. Joshi P, Chakraborty S, Dey S, Shanker V, Ansari ZA, Singh SP and Chakrabarti P (2011). Binding of choloroquine-conjugated gold nanoparticles with bovine serum albumin. J. Colloid Interface Sci. 355, 402-409.
44. Sonavane S and Chakrabarti P (2010). Prediction of active site cleft using support vector machines. J. Chem. Inform. Modeling, 50, 2266-2273.
45. Chatterjee T, Chakraborti S, Joshi P, Singh SP, Gupta V and Chakrabarti P (2010). The effect of zinc oxide nanoparticles on the structure of the periplasmic domain of the Vibrio cholerae ToxR protein. FEBS J. 277, 4184-4194.
46. Debnath A, Saha A, Gomes A, Biswas S, Chakrabarti P, Giri B, Biswas AK, Das Gupta S and Gomes A (2010). A lethal cardiotoxic-cytotoxic protein from the Indian monocellate cobra (Naja kaouthia) venom. Toxicon 56, 569-579.
47. Guharoy M and Chakrabarti P (2010). Conserved residue clusters at protein-protein interfaces and their use in binding site identification. BMC Bioinformatics 11: 286.
48. Dey S, Pal A, Chakrabarti P and Janin J (2010). The subunit interfaces of weakly associated homdimeric proteins. J. Mol. Biol. 398, 146-160.
49. Chakraborti S, Chatterjee T, Joshi P, Poddar A, Bhattacharyya B, Singh SP, Gupta V and Chakrabarti P (2010). Structure and activity of lysozyme on binding to ZnO nanoparticles. Langmuir, 26(5), 3506-3513.
50. Bahadur RP and Chakrabarti P (2009). Discriminating the native structure from decoys using scoring functions based on the residue packing in globular proteins. BMC Struct. Biol. 9: 76.
51. Guharoy M and Chakrabarti P (2009). Empirical estimation of the energetic contribution of individual interface residues in structures of protein-protein complexes. J. Comput. Aided Mol. Des. 23, 645-654.
52. Mukherjee D, Saha RP and Chakrabarti P (2009). Structural and unfolding features of HlyT, a tetrameric LysR type transcription regulator of Vibrio cholerae. Biochim. Biophys. Acta, 1794, 1134-1141.
53. Sonavane S and Chakrabarti P (2009). Cavities in protein-DNA and protein-RNA interfaces. Nucleic Acids Res. 37, 4613-4620.
54. Joshi P, Chakraborti S, Chakrbarti P, Haranath D Shanker V, Ansari ZA, Singh SP and Gupta V (2009). Role of surface adsorbed anionic species in antibacterial activity of ZnO quantum dots against Escherichia coli. J. Nanosci. Nanotechnol. 9, 6427-6433.
55. Pal A, Bahadur RP, Ray PS and Chakrabarti P (2009). Accessibility and partner number of protein residues, their relationship and a webserver, ContPlot for their display. BMC Bioinformatics 10: 103.
56. Pal A, Bhattacharyya R, Dasgupta M, Mandal S and Chakrabarti P (2009). IntGeom: a server for the calculation of the interaction geometry between planar groups in proteins. J. Proteomics & Bioinformatics 2(1), 60-63.
57. Biswas S, Guharoy M and Chakrabarti P (2009). Dissection, residue conservation, and structural classification of protein-DNA interfaces. Proteins 74(3), 643-654.
58. Sonavane S and Chakrabarti P (2008). Cavities and atomic packing in protein structures and interfaces. PLoS Comput. Biol. 4(9): e1000188.
59. Dasgupta B and Chakrabarti P (2008). pi-Turns: types, systematics and the context of their occurrence in protein structures. BMC Struct. Biol. 8: 39.
60. Biswas S, Guharoy M and Chakrabarti P (2008). Structural segments and residue propensities in protein-RNA interfaces: comparison with protein-protein and protein-DNA complexes. Bioinformation 2(10), 422-427.
61. Janin J, Bahadur RP and Chakrabarti P (2008). Protein-protein interaction and quaternary structure. Q. Rev. Biophys. 41 (2) 133-180.
62. Chatterjee T, Saha RP and Chakrabarti P (2007). Structural studies on Vibrio cholerae ToxR periplasmic and cytoplasmic domains. Biochim. Biophys. Acta 1774, 1331-1338.
63. Dasgupta B, Chakrabarti P and Basu G (2007). Enhanced stability of cis Pro-Pro peptide bond in Pro-Pro-Phe sequence motif. FEBS Letters, 581, 4529-4532.
64. Guharoy M and Chakrabarti P (2007). Secondary structure based analysis and classification of biological interfaces: identification of binding motifs in protein-protein interactions. Bioinformatics, 23, 1909-1918.
65. Chakrabarti P and Bhattacharyya R (2007). Geometry of nonbonded interactions involving planar groups in proteins. Prog. Biophys. Mol. Biol. 95, 83-137.
66. The NMITLI-BioSuite Team (Vidyasagar et al.) (2007). BioSuite: a comprehensive bioinformatics software package (A unique industry-academia collaboration). Curr. Sci. 92, 29-38.
67. Janin J, Rodier F, Chakrabarti P and Bahadur R (2007). Macromolecular recognition in the Protein Data Bank. Acta Crystallogr. D63, 1-8.
68. Pal A, Chakrabarti P, Bahadur R, Rodier F and Janin J (2007). Peptide segments in protein-protein interfaces. J. Biosci. 32, 101-111.
69. Saha RP, Bhattacharyya R and Chakrabarti P (2007). Interaction geometry involving planar groups in protein-protein interfaces. Proteins, 67, 84-97.
70. Saha, RP and Chakrabarti P (2006). Molecular modeling and characterization of Vibrio cholerae transcription regulator HlyU. BMC Struct. Biol. 6, 24.
71. Saha RP, Bahadur R, Pal A, Mandal S and Chakrabarti P (2006). ProFace: a server for the analysis of the physicochemical features of protein-protein interfaces. BMC Struct. Biol. 6, 11.
72. Raichaudhuri A, Bhattacharyya R, Chaudhuri S, Chakrabarti P and DasGupta M (2006). Domain analysis of a groundnut calcium-dependent protein kinase: nuclear localization sequence in the junction domain is coupled with nonconsensus calcium binding domains. J. Biol. Chem. 281, 10399-10409.
73. Saha RP, Basu G and Chakrabarti P (2006).Cloning, expression, purification, and characterization of Vibrio cholerae transcriptional activator, HlyU. Protein Expression and Purification, 48, 118-125.
74. Saha RP and Chakrabarti P (2006). Parity in the number of atoms in residue composition in proteins and contact preferences. Curr. Sci. 90, 558-561.
75. Singha S, Lahiri T, Dasgupta AK and Chakrabarti P (2006). Structural classification of protein using surface roughness index. Online Journal of Bioinformatics, 7(2), 74-84.
76. Guharoy M and Chakrabarti P (2005). Conservation and relative importance of residues across protein-protein interfaces. Proc. Natl. Acad. Sci. USA, 102, 15447-15452.
77. Datta AB, Panjikar S, Weiss MS, Chakrabarti P and Parrack P (2005). Structure of l CII: implications for recognition of direct-repeat DNA by an unusual tetrameric organization. Proc. Natl. Acad. Sci. USA, 102, 11242-11247.
78. Saha RP, Bahadur RP and Chakrabarti P (2005). Inter-residue contacts in proteins and protein-protein interfaces and their use in characterizing the homodimeric interface. J. Proteome Res. 4, 1600-1609.
79. Rodier F, Bahadur RP, Chakrabarti P and Janin J (2005). Hydration of protein-protein interfaces. Proteins, 60, 36-45.
80. Pal L, Dasgupta B and Chakrabarti P (2005). 310-helix adjoining a-helix and b-strand: sequence, structural features and their conservation. Biopolymers, 78, 147-162.
81. Bhattacharyya R, Pal D and Chakrabarti, P (2004). Disulfide bonds, their stereospecific environment and conservation in protein structures. Protein Eng. Design Selection, 17, 795-808.
82. Bahadur RP, Chakrabarti P, Rodier F and Janin J (2004). A dissection of specific and non-specific protein-protein interfaces. J. Mol. Biol. 336, 943-955.
83. Dasgupta B, Pal L, Basu G and Chakrabarti P (2004). Expanded turn conformations: characterization and sequence-structure correspondence in a-turns with implications in helix folding. Proteins, 55, 305-315.
84. Bhattacharyya R and Chakrabarti P (2003). Stereospecific interactions of proline residues in protein structures and complexes. J. Mol. Biol. 331, 925-940.
- The Jagadis Chandra Bose Medal, INSA , 2016
- Distinguished Alumnus Award, IIT Kharagpur, 2012
- Fellow, TWAS (The World Academy of Sciences), 2011
- JC Bose National Fellow , 2007
- President, Asian Crystallographic Association (AsCA), 2013
- Fellow, Indian National Science Academy, 2006
- The Bires Chandra Guha Memorial Lecture, INSA, 2011
- Prof. YT Thathachari Prestigious Award for Science, 2005
- Fellow, Indian Academy of Sciences, 1998
- Fellow, The National Academy of Sciences, 2006
Courses offered on: Protein conformation, Bioinformatics, Protein Crystallography
|Jesmita Dhar||SRF||Bioinformatics Centre||Centenary||25693273||jesmita|
|Sudipta Bag||SRF(Extended)||Bioinformatics Centre||Centenaryfirstname.lastname@example.org|
1) Ms. Shamila Sarwar (SRF); email@example.com
2) Ms. Jesmita Dhar (SRF); firstname.lastname@example.org
3) Mr. Supriyo Bera (SRF); email@example.com
4) Dr. Avisek Mondal (Post-doc); firstname.lastname@example.org
5) Dr. Swapan Jana (Post-doc); email@example.com
Besides I am the mentor of Dr. Tanaya Chatterjee (firstname.lastname@example.org), who has her own independent DST Women's Scientist Project