Publications

  • 66- Vishwakarma, P., Puri, S., Banerjee, M., Chang, C. Y., Chang, C. C., & Chaudhuri, T. K. (2024). Deciphering the Thermal Stability of Bacteriophage MS2-Derived Virus-like Particle and Its Engineered Variant. , 10(8), 4812-4822. ACS Biomaterials Science & Engineering 2024. (Pdf)

  • 65- Srivastava, V., Bandhu, S., Mishra, S., Chaudhuri, T. K. (2024). Serratiopeptidase exhibits antibiofilm activity through the proteolytic function of N-terminal domain and versatile function of the C-terminal domain. https://doi.org/10.1016/j.bbapap.2024.141046 (BBA)-Proteins and Proteomics, 2024. (Pdf)

  • 64- Srivastava, V., Bandhu, S., Mishra, S. and Chaudhuri, T.K. (2024), Calcium-induced structural transitions are central to the folding, function, and processing of serratiopeptidase zymogen into mature form. FEBS J. https://doi.org/10.1111/febs.17090 FEBS J. 2024. (Pdf)

  • 63- Anu Prakash, Mansi Marwah, Devanshu Mehta, Tapan K. Chaudhuri, Himanshu Ojha & Paban K Agrawala (2023) Biophysical studies of the binding of histone deacetylase inhibitor (Trichostatin-A) with bovine serum albumin, Journal of Biomolecular Structure and Dynamics, DOI: 10.1080/07391102.2023.2246071 JOURNAL OF BIOMOLECULAR STRUCTURE AND DYNAMICS 2023. (Pdf)

  • 62- Piplani, B., Kumar, C. M. S., Lund, P. A. & Chaudhuri, T. K. (2023). Mycobacterial chaperonins in cellular proteostasis: Evidence for chaperone function of Cpn60.1 and Cpn60.2-mediated protein folding. Molecular Microbiology, 120, 210–223. https://doi.org/10.1111/mmi.15109 Molecular Microbiology 2023. (Pdf)

  • 61- Mehta D, Singh H, Haridas V, Tapan K. Chaudhuri*. “Molecular Insights into the Inhibition of Dialysis-Related β2m Amyloidosis Orchestrated by a Bispidine Peptidomimetic Analogue. Biochemistry”. 2022. (Pdf)

  • 60- Ankit Pal, & Tapan K. Chaudhuri*, (2022). “Enhancement in the production of recombinant human paraoxonase 1 in Escherichia Coli: A comprehensive approach of cellular engineering and optimisation of protein folding process in vitro”. International Journal of Biological Macromolecules. (Pdf)

  • 59- Ravitchandirane, G., Bandhu, S. & Tapan K. Chaudhuri* “Multimodal approaches for the improvement of the cellular folding of a recombinant iron regulatory protein in E. coli”. Microb Cell Fact 21, 20 (2022).(Pdf)

  • 58- S Bandhu, A Srivastava, D Ghosh, Tapan K. Chaudhuri “Yeast Single Cell Oils from Bioresources: Current Developments in Production and Applications”. 2020, Current Sustainable/Renewable Energy Reports, 1-12.(Pdf)

  • 57- G Singh, R Mishra, G Goel, T Chaudhuri, 2020, “Old Arsenal to Combat New Enemy: Repurposing of Commercially Available FDA Approved Drugs Against Main Protease of SARS-CoV2”. Chemrxiv, 10.26434/chemrxiv.13032578.v1(Pdf)

  • 56- Vishal Srivastava, Shivam Mishra, and Tapan K.Chaudhuri.*,"Enhanced production of recombinant serratiopeptidase in Escherichia coli and its characterization as a potential biosimilar to native biotherapeutic counterpart.", Microb Cell Fact. 18:215(2019). (Pdf)

  • 55- Bhaskar K. Chatterjee, Abhilash Jayaraj, Vinay Kumar, Brian Blagg, Rachel Davis, B. Jayaram, Shashank Deep , Tapan K. Chaudhuri.*,"Stimulation of heat shock protein 90 chaperone function through binding of a novobiocin analog KU-32.",J Biol Chem.294(16) (2019), pp 6450-6467. (Pdf)

  • 54- Sarita Puri, Tapan K. Chaudhuri*,"Improvement of structural stability and functional efficiency of chaperonin GroEL mediated by mixed salt.", Int J Biol Macromol. 129(2019), pp 792-798. (Pdf)

  • 53- Sarita Puri, Tapan K. Chaudhuri*, "Inter and intra-subunit interactions at the subunit interface of chaperonin GroEL are essential for its stability and assembly.",Biochim Biophys Acta Proteins Proteom.1867(3)(2019), pp 331-343. (Pdf)

  • 52- Vipul Kumar and Tapan K. Chaudhuri*, "Spontaneous refolding of the large multidomain protein malate synthase G proceeds through misfolding traps", Journal of Biological Chemistry, 293(2018), pp 13270-13283. (Pdf)

  • 51- Neha Jain, Tim J. Knowles, Peter A. Lund, and Tapan K. Chaudhuri*, "Minichaperone (GroEL191-345) mediated folding of MalZ proceeds by binding and release of native and functional intermediates.", Biochim Biophys Acta Proteins Proteom., 1866(9)(2018), pp 941-951. (Pdf)

  • 50- Ashish Sharma, M. Saqib, J. A. Sheikh, N. Z. Ehtesham, S. Bhaskar, S. E. Hasnain and Tapan K. Chaudhuri*, "Mycobacterium indicus pranii protein MIP_05962 induces Th1 cell mediated immune response in mice.", Int J Med Microbiol., 308(8)(2018), pp 1000-1008. (Pdf)

  • 49- Md. Ashif Shah, Saroj Mishra, Tapan K. Chaudhuri*, "Marginal stability drives irreversible unfolding of large multi-domain family 3 glycosylhydrolases from thermo-tolerant yeast." Int J Biol Macromol. 108(2018), pp 1322-1330. (Pdf)

  • 48- Bhaskar Chatterjee, Sarita Puri, Ashima Sharma, Ashutosh Pastor, Tapan K. Chaudhuri*, "Molecular Chaperones: Structure-Function Relationship and their Role in Protein Folding", book chapter:Asea A., Kaur P. (eds) Regulation of Heat Shock Protein Responses. Heat Shock Proteins, vol 13. Springer, Cham(2018). (Pdf)

  • 47- Ashima Sharma, Tapan K. Chaudhuri*, Physicochemical characterization of E. coli -derived human serum albumin and its comparison with the human plasma counterpart reveals it as a promising biosimilar, Journal of Biotechnology, 7;274(2018):1-8. (Pdf)

  • 46- Ashima Sharma, Tapan K. Chaudhuri*, Revisiting Escherichia coli as microbial factory for enhanced production of human serum albumin, Microbial Cell Factories 16:173(2017). (Pdf)

  • 45- Ashish Sharma, M. A. Equbal, S. Pandey, Javaid A. Sheikh, Nasreen Z. Ehtesham, Seyed E. Hasnain*, and T.K. Chaudhuri*, Immunodominant protein MIP_05962 from Mycobacterium indicus pranii displays chaperone activity, FEBS Journal (2017). (Pdf)

  • 44- Sarita Puri and Tapan K. Chaudhuri*," Folding and Unfolding Pathway of Chaperonin GroEL Monomer and Elucidation of Thermodynamic Parameters ", International Journal of Biological Macromoleules, 96 (2017), 713–726. (Pdf)

  • 43- Ashutosh Pastor, Amit K. Singh, Mark T. Fisher, Tapan K. Chaudhuri, "Protein folding on Biosensor tips: Folding of Maltodextrin glucosidase monitored by its interactions with GroEL", FEBS Journal,283(16), August 2016, 3103-14. (Pdf)

  • 42- Ashutosh Pastor, Amit K. Singh, Prakash K. Shukla, Md. Javed Equbal, Shikha T. Malik, Tej P. Singh, Tapan K. Chaudhuri, Role of N-terminal region of Escherichia coli Maltodextrin Glucosidase in folding and function of the protein, BBA - Proteins and Proteomics, 1864 (9), September 2016, 1138–1151. (Pdf)

  • 41- Manish Bhuwan, Naresh Arora, Ashish Sharma, Mohd Khubaib, Saurabh Pandey, Tapan K. Chaudhuri, Syed Ehtesham Hasnain, Nasreen Zafar Ehetesham, Interaction of Mycobacterium tuberculosis Virulence Factor RipA with Chaperone MoxR1 Is required for transport through the TAT Secretion system. mBio, January/February 2016, vol7, issue 1 e02259-15. (Pdf)

  • 40- Saurabh Pandey, Ashish Sharma, Manish Bhuwan, Mohd Khubaib, deeksha, Tapan K. Chaudhuri, Syed Ehtesham Hasnain, Nasreen Zafar Ehetesham, Mycobacterium tuberculosis peptidyl-prolyl isomerases also exhibit chaperone like activity in-vitro and in-vivo. PLoS One. 2016 16;11(3):e0150288. (Pdf)

  • 39- Megha Goyal and Tapan K. Chaudhuri, GroEL-GroES assisted folding of multiple recombinant proteins simultaneously over-expressed in Escherichia coli.The Int. Journal of Biochem and Cell Biology, 64 (2015) 277–286. (Pdf)

  • 38- Sailendra Mahanta, Subhankar Paul, Ankit Srivastava , Ashutosh Pastor ,Bishwajit Kundu, and Tapan K. Chaudhuri, Stable self-assembled nanostructured hen egg white lysozyme exhibits strong anti-proliferative activity against breast cancer cells, Colloids and Surfaces B: Biointerfaces, 130 (2015) 237–245. (Pdf)

  • 37- Megha Goyal, Tapan K. Chaudhuri*, Kunihiro Kuwajima, Irreversible Denaturation of Maltodextrin Glucosidase Studied by Differential Scanning Calorimetry, Circular Dichroism, and Turbidity Measurements. PlosOne, (2014) 9(12): e115877. (Pdf)

  • 36- Vinay Dahiya and Tapan K. Chaudhri* "GroEL/ES acccelerates the refolding of a multi-domain protein through modulating on pathway intermediates". Journal of Biological Chemistry, 289(1), 2014, pp 286-298. (Pdf)

  • 35- Madhuri Suragani, Varma D. Aadinarayana, Aleem B. Pinjari, Karunakar Tanneeru, Lalitha Gururprasad, Sharmishtha Banerjee, Saurabh Pandey, Tapan K. Chaudhuri* and Nasreen Z. Ehtesham "Human Resistin, a Pro-inflammatory cytokine, shows chaperone like activity". PNAS(USA), December 17, 2013, Vol 110, no. 51, 20461- 20472. (Pdf)

  • 34- Vinay Dahiya and Tapan K. Chaudhuri* "Functional intermediate in the refolding of a large and multidomain protein Malate Synthase G". Biochemistry (ACS Publications) ,2013,52,4517-4530. (Pdf)

  • 33- Mahesh S. Chandak, Takashi Nakamura, Toshio Takenaka, Tapan K. Chaudhuri, Maho Yagi-Utsumi, Jin Chen, Koichi Kato and Kunihiro Kuwajima. "The use of spin desalting columns in DMSO-Quenched H/D-exchange NMR experiments". Protein Science 2013, 22(4):486-91. (Pdf)

  • 32- Mahesh S. Chandak, Takashi Nakamura, Koki Makabe, Toshio Takenaka, Atsushi Mukaiyama, Tapan K. Chaudhuri, Jin Chen, Koichi Kato, and Kunihiro Kuwajima " The H/D-exchange Kinetics of the Escherichia coli Co-chaperonin GroES Studied by 2D-NMR and DMSO-Quenched Exchange Methods". Journal of Molecular Biology, 2013, 425(14):2541-60. (Pdf)

  • 31- Vipul Kumar, Ankita Punetha, Durai Sundar*, and Tapan K. Chaudhuri*, "In silico engineering of aggregation prone recombinant proteins for substrate recognition by chaperonin GroEL". BMC Genomics, 2012, 13(suppl 7):S22. (Pdf)

  • 30- Mohammad Asif Shah, Tapan Kumar Chaudhuri and Saroj Mishra, Strategy for purification of aggregation prone ß-glucosidases from cell wall of yeast : a preparative scale approach. New Biotechnology, 15;29(3):311-20, February 2012. (Pdf)

  • 29- Md. Asif Shah, Saroj Mishra, and Tapan K. Chaudhuri. Structural stability and unfolding transition of β-glucosidases: A comparative investigation on isozymes from a thermo-tolerant yeast. European Biophysics Journal (2011) 40:877-889.(Pdf)

  • 28- Aditi Maheshwari, Vikash K. Verma and Tapan K. Chaudhuri*. Equilibrium and kinetics of the Unfolding and Refolding Escherichia coli Malate Synthase G monitored by circular dichroism and fluorescence spectroscopy. Biochimie, 92 , 491-498, (2010). (Pdf)

  • 27- Parul Gupta, Saroj Mishra,and Tapan K. Chaudhuri*. Reduced stability and enhanced surface hydrophobicity drive the binding of apo-aconitase with GroEL during chaperone assisted refolding. The International Journal of Biochemistry and cell Biology, 42 683–692, (2010). (Pdf)

  • 26- Jai Mittal, Gayathri Ravitchandirane, Tapan K. Chaudhuri, Pratima Chaudhuri (Chattopadhyay). Structure-activity correlationship and folding of recombinant Escherichia coli dihydro folate reductase (DHFR) enzyme through biochemical and biophysical approaches. Journal of Biophysical Chemistry, Vol.1, No.2, 105-112 (2010). (Pdf)

  • 25- Tapan K. Chaudhuri* , Verma, V.K., Maheshwari, A.. GroEL assisted folding of large polypeptide substrates in Escherichia col: Present scenario and assignments for the future. Progress in Biophysics and Molecular Biology 99(1):42-50 (2009). (Pdf)

  • 24- Parul Gupta, Anand Ghosalkar, Saroj Mishra and Tapan K. Chaudhuri* Enhancement of over expression and chaperone assisted yield of folded recombinant aconitase in Escherichia coli in bioreactor cultures. Journal of Bioscience and Bioengineering; 107(2):102-7 (2009). (Pdf)

  • 23- Jaskaran Lamba, Subhankar Paul, Vivek Hasija, Ruchi Aggarwal and Tapan K. Chaudhuri* . Monitoring Protein Folding and Unfolding Pathway through Surface Hydrophobicity Changes using Fluorescence and Circular Dichroism Spectroscopy . Biochemistry (Moscow) Apr; 74(4):393-8 (2009). (Pdf)

  • 22- Subhankar Paul, Suman Jha, Madhuchhanda Kundu, Kali P. Das, Saroj Mishra and Tapan K. Chaudhuri*. Unfolding studies of Escherichia coil maltodextrin glucosidase monitored by flurescence spectroscopy. Journal of Biological Physics, Dec; 34(6):539-50 (2008). (Pdf)

  • 21- Subhankar Paul and Tapan K. Chaudhuri*. Chaperone mediated solubilization of 69-kDa recombinant maltodextrin glucosidase in Escherichia coli. Journal of Applied Microbiology (2008) , Jan; 104(1):35-41. (Pdf)

  • 20- Salony Senapati,Saroj Mishra, Tapan K. Chaudhuri ,Virendra S Bisaria, Neha Garg, Meenu Chhabra, Richa Barnawal. Laccase of cyathus bulleri: structural, catalytic characterization and expression in Escherichia coli. BBA - Proteins and Proteomics , 1784(2):259-68 (2008). (Pdf)

  • 19- Subhankar Paul, Sashikala Punam and Tapan K. Chaudhuri* . Chaperone-assisted refolding of Escherichia coli maltodextrin glucosidase. FEBS Journal 274 (22) , 6000–6010 (2007). (Pdf)

  • 18- Subhankar Paul, Chanpreet Singh, Saroj Mishra and Tapan K Chaudhuri.* The 69-kDa Escherichia coli Maltodextrin Glucosidase does not Get Encapsulated Underneath GroES and Folds through trans Mechanism During GroEL/GroES Assisted Folding. The FASEB Journal Vol.21(11) 2874-2885,(2007). (Pdf)

  • 17- Nitharwal, RamGopal; Paul, Subhankar; Dar, Mohd; Choudhury, Nirupam; Soni, Rajesh; Prusthy, Dhaneswar; Sinha, Sukrat; Keshav, Tara; Mukhopadhyay, Gauranga; Chaudhuri, Tapan K.,Gourinath, Samudrala; Dhar, Suman.The Domain structure of Helicobacter Pylori DNA b Helicase : The N- terminal domain can be dispensable for helicase activity where as the extreme C- terminal region is essential for its function. Nucleic Acid research (NAR), Vol 35 (9) pp 2861-2874, (2007). (Pdf)

  • 16- Eli Chapman, George W. Farr, Renata Usaite, Krystyna Furtak, Wayne A. Fenton, Tapan K. Chaudhuri, Elise R. Hondorp, Rowena G. Matthews, Sharon G. Wolf, John R. Yates, Marc Pypaert, and Arthur L. Horwich.Global Aggregation of Newly translated Proteins in an E.coli Strain Deficient of the Chaperonin GroEL.Proceedings of National Academy of Science (PNAS,USA) Vol.103, No.43, pp15800-15805, (2006). (Pdf)

  • 15- Parul Gupta, Nishtha Aggarwal, Pragya Batra, Saroj Mishra and Tapan K. Chaudhuri*. Co-expression of chaperonin GroEL/GroES enhances in vivo folding of yeast mitochondrial aconitase and alters the growth characteristics of Escherichia coli. The International Journal of Biochemistry and cell Biology, Vol. 38 (11), 1975-1985, (2006). (Pdf)

  • 14- Jana S, Chaudhuri TK and Deb JK. The effects of guanidine hydrochloride on the conformation and enzyme activity of streptomycin adenylyltransferase monitored by circular dichroism and fluorescence spectroscopy. Biochemistry (Moscow),71 (11), pp1230-1237, (2006). (Pdf)

  • 13- Chaudhuri T.K* and Paul S. Protein misfolding diseases and chaperone based therapeutic approaches. FEBS Journal, Vol 273, pp 1331-1349, (2006). (Pdf)

  • 12- Roy Pranita, Mishra S and Chaudhuri TK. Cloning, sequence analysis and characterization of a novel b-glucosidase-like activity from Pichia etchellsii Biochemical and Biophysical Research communications; 336 299–308, (2005). (Pdf)

  • 11- Chaudhuri TK* and Gupta P. Factors Governing the Substrate recognition by GroEL chaperone: A sequence correlation Approach Cell stress and Chaperones (2005), Vol.10 (1) pp 24-36. (Pdf)

  • 10- Farr G.W., Fenton WA., Chaudhuri TK., Clare DK., Saibil HR, and Horwich AL. Folding with and without encapsulation by cis and trans-only complexes. The EMBO Journal Vol. 22 No. 13 pp. 3220-3230, 2003. (Pdf)

  • 9- Chaudhuri TK, Farr GW, Fenton WA, Rospert S, and Horwich AL. , GroEL/GroES-mediated Folding of a Protein Too Large To Be Encapsulated CELL , vol.107, 235-246, October 19, (2001). (Pdf)

  • 8- Horwich AL, Farr GW, Fenton WA, Furtak K, Chaudhuri TK, Bertelsen E, Fiaux J, Riek R, Wuthrich K. "GroEL-GroES mediated protein folding" Molecular Biology of the Cell, Volume 12, Pages : 399A-399A, Nov 2001, (Supplement of meeting abstract : 2195). (Pdf)

  • 7- Chaudhuri TK, Arai M, Terada TP, Ikura T, Kuwajima K. Equilibrium and kinetic studies on folding of the authentic and recombinant forms of human alpha-lactalbumin by circular dichroism spectroscopy. Biochemistry,39:15643-51,(2000). (Pdf)

  • 6- Chaudhuri TK, Horii K, Yoda T, Arai M, Nagata S, Terada TP, Uchiyama H, Ikura T, Tsumoto K, Kataoka H, Matsushima M, Kuwajima K, Kumagai I. Effect of the extra n-terminal methionine residue on the stability and folding of recombinant alpha-lactalbumin expressed in Escherichia coli. Journal of Molecular Biology, 285:1179-94(1999). (Pdf)

  • 5- Yoda, T., Saito, M., Arai, M. Horii, K., Tsumoto, K., Matsushima, M. Kumagai, I., Chaudhuri, T.K. and Kuwajima K.,"Kinetic folding reaction and Molecular dynamic simulations of alphalactalbumin. Old and New Views of Protein Folding", Kuwajima, K and Arai, M. eds. 155-161.(1999). (Pdf)

  • 4- Chaudhuri T. K*.,"Refolding kinetics of partially reduced and S-carboxymethylated trypsin-subtilisin inhibitor from marine turtle eggwhite",Biochemistry Molecular Biology International. 41:1077-84, (1997). (Pdf)

  • 3- Chaudhuri T. K., Sinha N. K.,"Refolding of trypsin-subtilisin inhibitor from marine turtle eggwhite", Journal of Protein Chemistry15:315-20, (1996). (Pdf)

  • 2- Sil P. C., Chaudhuri T. K., Sinha N. K., "Basic trypsin-subtilisin inhibitor from marine turtle egg white: hydrodynamic and inhibitory properties.", Journal of Protein Chemistry. 12:71-8, (1993). (Pdf)

  • 1- Chaudhuri T. K., Das K. P., Sinha N. K., "Surface hydrophobicity of a low molecular weight basic trypsin subtilisin inhibitor from marine turtle eggwhite", Journal of Biochemistry (Tokyo) 113:729-33, (1993). (Pdf)

    • Publications in conferences / symposia

    • 1- Charu Thapliyal, Pratima Chaudhuri, Tapan K. Chaudhuri, The Influence of the Apical Domain of Groel Chaperone on the Kinetics and Thermodynamics of Zebrafish Dihydrofolate Reductase Under Thermal Stress. , Biophysical Journal 114:3; 413a.


    • 2- Vishal Srivastava, Tapan K. Chaudhuri, Extracellular Calcium Concentration Mediates Disorder To Order Transition And Functional Processing Of Serralysin; BEMS Reports. 2017; 3(2): 24-66. (Young Scientist and Best Poster Award).

    • 3- Shivam Mishra, vishal Srivastava, Tapan K. Chahudhuri, Utilizing α-Amylase as a Template to Design Novel Anti-biofilm Peptide Molecules., BEMS Reports. 2017; 3(2): 24-66.

    • 4- Chaperonin GroEL assisted folding of multiple aggregation prone proteins overexpressed simultaneously in Escherichia coli cytosol, pg 81, poster no. 21. EMBO Conference: The Biology of molecular chaperones: from molecules, organelles and cells to misfolding diseases. 8-13th May 2015, Heraklion, Crete, Greece.

    • 5- GroEL and GroES assisted protein folding in Escherichia coli: Mechanism and application . 17th International Biophysics Conference, October 30 -November 03, 2011, Beijing, China.

    • 6- Molecular Chaperone as cellular protein folding machines and potential therapeutic agent for protein misfolding disorders Proceedings of the NATIONAL SYMPOSIUM ON BIOMOLECULAR DRUG TARGETS & WORKSHOP ON CURRENT TRENDS IN BIOINFORMATICS. March 7-9, 2011, Aligarh Muslim University, India.

    • 7- Role of molecular chaperones GroEL and GroES in the Assisted folding pathway".Proceedings of National symposium on ORGANIC CHEMISTRY-IV (NSOC-IV): Modern trends and perspectives, Feb 2-3,2011, Jadavpur University.

    • 8- Structure-activity correlationship and conformational characterisation of streptomycin inactivating enzyme streptomycin adenylatetransferase (SMATase). Proceedings of the 3rd. International conference on Antimicrobial Resistance in Animals and the Environment. pp 109, Tours, France, 1-3rd June, 2009.

    • 9- An attempt at Understanding the Probable Reason of Binding of Apo-aconitase with GroEL during its Assisted Folding Pathway. Indian Biophysical Society Annual conference, IBS 2008. pp -1, CCMB Hyderabad 22-24 January, 2009.

    • 10- Mini -GroEL can assist in the in vivo and in vitro folding of large natural substrate proteins" Proceedings of the 5th. Open workshop Chemistry of Biological Processes Created by Water and Biomolecules page 66, Nara, Japan, January 24-25,, 2008.

    • 11- Substrate recognition and mode of action of GroEL in the assisted folding of non-native polypeptides. National Symposium on Biophysics: Trends in Biomedical Research. pp 55, IBS 2007, February 13-15,, AIIMS, New Delhi, 2007.

    • 12- Cis and trans folding mechanism in GroEL/GroES Assisted protein Folding International Conference on Structure and Dynamics: From Micro to Macro ; Department of Chemistry, University of Calcutta, India, 15-17th December 2006.
    • 13- GroEL/GroES Fold Large Substrate Proteins in Escherichia coli through Trans Mechanism, in the 75th. Annual Conference for the Society of Biological Chemists in India (SBC). JNU, New Delhi ; PP 84, 8-11December, 2006.

    • 14- Subhankar paul and Tapan K. Chaudhuri, Escherichia coli protein Maltodextrin Glucosidase (MalZ) folds through trans sided mechanism in the GroEL-GroES assisted pathway, in the 75th. Annual Conference for the Society of Biological Chemists in India (SBC). JNU, New Delhi 8-11 December, PP 147. (Best poster award, 2006.)

    • 15- Tapan K. Chaudhuri, GroEL-GroES assisted and unassisted in vivo and in vitro folding of a large recombinant Escherichia coli protein Maltodextrin Glucosidase: Molecules, Interactions and Design: A Biophysical Perspective , National symposium, IBS 2006, Kolkta, India, pp 93. (2006).

    • 16- Tapan K. Chaudhuri, Chaperone Mediated Protein Folding in Vivo can be a solution to the Production of Recombinant Proteins in Escherichia coli; Microbial Diversity: Current perspective and potential applications, pp-36-37, International conference, April 16-18, New Delhi(India), (2005).

    • 17- Chaudhuri T. K., Chaperone Assisted Folding of Large Substrate Proteins, Proceedings of National Symposium of Biophysics, IIT Roorkee, India, P. L41, (2003).

    • 18- Chaudhuri T. K., Horii K., Yoda T., Arai M., Nagata S., Terada T. P., Uchiyama H., Ikura T., Tsumoto K., Kataoka H., Matsushima M., Kuwajima K., Kumagai I., Role of terminal methionine residue in the structure and stability of recombinant alpha lactalbumin proceedings of the Twelfth Symposium of Protein Society, USA, San diego, California, USA, (1998).

    • 19- Chaudhuri T.K and Sinha N.K., Refolding study of basic trypsing subtilisin inhibitor from marine turtle eggwhite , proceedings of the XVIth. International congress of Biochemistry and Molecular Biology, New Delhi, India, (1992).

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