Krishnananda Chattopadhyay

Dr. Krishnananda Chattopadhyay

Principal Scientist

Ph.D, Tata Institute of Fundamental Research, 2000
Research Associate (1999-2005), Washington University School of Medicine, St. Louis, USA ,
Senior Scientist (2005-2006), Pfizer Global Biologics, St. Louis, USA

Structural Biology and Bioinformatics Division

    • Fluorescence Correlation Spectroscopy and Protein Folding
    • Protein Stability and Aggregation
    1. Sangeeta Kundu (Research Scientist) (
    2. Sunny Sharma (SRF) (
    3. Nidhi Joshi (Project Assistant) (
    4. Sujit Basak (SRF) (
    5. Suparna Sarkar (SRF) (
    6. Simanta Sarani Paul (SRF) (
    7. Pallabi Sil (SRF) (
    8. Amrita Kundu (JRF) (
    9. Sourav Chowdhury (JRF) (
    10. Sumanta Ghosh (JRF) (
    1. Sharma, S., Sarkar, S., Paul, S.S., Roy, S. & Chattopadhyay, K. A small molecule chemical chaperone optimizes its unfolded state contraction and denaturant like properties. Sci. Rep. 3, 3525; DOI:10.1038/srep03525 (2013).
    2. Basak S, Chattopadhyay K. Fluorescence Correlation Spectroscopy Study on the Effects of the Shape and Size of a Protein on Its Diffusion Inside a Crowded Environment. Langmuir. 2013 Nov 14. [Epub ahead of print]
    3. Nidhi Joshi , Anindita Mukhopadhyay , Sujit Basak , Goutam De , and Krishnananda Chattopadhyay. Surface Coating Rescues Proteins from Magnetite Nanoparticle Induced Damage. Part. Part. Syst. Charact. 2013, 30, 683–694
    4. Sunny Sharma, Nikhil Pathak, Krishnananda Chattopadhyay. Osmolyte induced stabilization of protein molecules: A Brief Review, Journal of Proteins and Proteomics. 2012; 3(2):129-139.
    5. Ghosh R, Mukherjee M, Chattopadhyay K, Ghosh S. Unusual optical resolution of all four tryptophan residues in MPT63 protein by phosphorescence spectroscopy: assignment and significance. J Phys Chem B. 2012 Oct 18;116(41):12489-500.
    6. Haldar, S., & Chattopadhyay, K. (2012) The interconnection of salt induced hydrophobic compaction and secondary structure formation depends on solution conditions: revisiting early events of protein folding at single molecule resolution. Journal of Biological Chemistry VOL. 287, NO. 14, pp. 11546–11555, March 30, 2012
    7. Haldar, S., Paul, S. S., Joshi, N., Dasgupta, A., Chattopadhyay, K., (2012) The Presence of the Iron-Sulfur Motif Is Important for the Conformational Stability of the Antiviral Protein, Viperin. Plos One Volume 7 | Issue 2 | e31797.
    8. Lahiri, S., Basu, A., Sengupta, S., Banerjee, S., Dutta, T., Soren, D., Chattopadhyay, K., Ghosh, A. K., Purification and characterization of a trehalase–invertase enzyme with dual activity from Candida utilis (2012) Archives of Biochemistry and Biophysics Volume 522, Issue 2, Pages 90–99.
    9. Mukhopadhyay A, Joshi N, Chattopadhyay K, De G. (2011) A facile synthesis of PEG-coated magnetite (Fe3O4) nanoparticles and their prevention of the reduction of cytochrome c. ACS Appl Mater Interfaces. 2012 Jan;4(1):142-9. Epub 2011 Dec 9.
    10. Sen, T., Mandal, S., Haldar, S., Chattopadhyay, K., and Patra, A., (2011) J. Phys. Chem. C, 115 (49), pp 24037–24044.
    11. Haldar, S., & Chattopadhyay, K. (2011) Effects of arginine and other solution additives on the self-association of different surfactants: an investigation at single molecule resolution. Langmuir 27, 5842-5849
    12. Mukhopadhyay, A, Basak, S., Das, JK, Chattopadhyay, K. & De, G (2010) Ag-TiO2 nanoparticle co-doped SiO2 films on ZrO2 barrier-coated glass substrates with antibacterial activity in ambient condition. ACS Appl Mater Interfaces 9, 2540-6.
    13. Haldar, S, Mitra, S. & Chattopadhyay, K (2010) The role of the protein stabilizers on the conformations of the unfolded states and its early folding kinetics: An investigation at single molecular resolution. Journal of Biological Chemistry 285, 25314-23.
    14. Ghosh, R., Sharma, S. & Chattopadhyay, K.(2009) Effect of Arginine on Protein Aggregation Studied by Fluorescence Correlation Spectroscopy and Other Biophysical Methods, Biochemistry 48 (5), 1135 – 1143.
    15. Chattopadhyay, K. & Frieden, C. (2006) Steady State and Time-resolved fluorescence studies of the intestinal fatty acid binding proteins, Proteins 63, 327-335.
    16. Chattopadhyay, K., Elson, E. L., & Frieden, C. (2005) Measurements of microsecond dynamics of the unfolded state by using fluorescence methods, Proc. Natl. Acad. Sci (USA) 102, 2385-2389.
    17. Chattopadhyay, K., Saffarian, S., Elson, E. L., & Frieden, C, (2005) Measuring unfolding of proteins in the presence of denaturant using fluorescence correlation spectroscopy. Biophysical Journal 88, 1413-1422.
    18. Chattopadhyay, K., & Mazumdar, S. (2003) Stabilization of partially folded states of cytochrome c in aqueous micelles: effects of ionic and hydrophobic interactions. Biochemistry 42, 14606-14613.
    19. Chattopadhyay, K.; Saffarian, S.; Elson, E. L.; & Frieden, C. (2002) Measurement of microsecond dynamic motion in the intestinal fatty acid binding protein by using fluorescence correlation spectroscopy. Proc. Natl. Acad. Sci. (USA), 99, 14171 – 14176.
    20. Frieden, C.; Chattopadhyay, K.; & Elson, E.L; (2002) What Fluorescence Correlation Spectroscopy can tell us about unfolded state of a protein. Adv. Prot. Chem., 62, 91-109.
    21. Chattopadhyay, K; Das, T. K; Majumdar, A; & Mazumdar, S (2002) NMR studies on interaction of lauryl maltoside with cytochrome c oxidase: a model for surfactant interaction with the membrane protein. J. Inor. Biochem 91, 116-124.
    22. Chattopadhyay, K.; Zhong, S.; Yeh, S. R.; Rousseau, D., L; & Frieden, C. (2002) The Intestinal Fatty Acid Binding Protein: the role of turns in fast and slow folding processes. Biochemistry 41, 4040-4047.
    23. Chattopadhyay, K.; & Mazumdar, S. (2001) Direct electrochemistry of heme proteins: effect of electrode surface modification by neutral surfactants. Bioelectrochemistry 53, 17-24.
    24. Chattopadhyay, K.; & Mazumdar, S. (2000) Structural and conformational stability of horseradish peroxidase: effect of temperature and pH. Biochemistry 39, 263-270.
    25. Chattopadhyay, K.; &Mazumdar, S. (1999) Direct electrochemical oxidation of horseradish peroxidase: cyclic voltammetric and spectroelectrochemical studies. New J Chem 23, 137-139.