Dr. Krishnananda Chattopadhyay
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
- Fluorescence Correlation Spectroscopy and Protein Folding
- Protein Stability and Aggregation
- Sangeeta Kundu (Research Scientist) (firstname.lastname@example.org)
- Sunny Sharma (SRF) (email@example.com)
- Nidhi Joshi (Project Assistant) (firstname.lastname@example.org)
- Sujit Basak (SRF) (email@example.com)
- Suparna Sarkar (SRF) (firstname.lastname@example.org)
- Simanta Sarani Paul (SRF) (email@example.com)
- Pallabi Sil (SRF) (firstname.lastname@example.org)
- Amrita Kundu (JRF) (email@example.com)
- Sourav Chowdhury (JRF) (firstname.lastname@example.org)
- Sumanta Ghosh (JRF) (email@example.com)
- 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).
- 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]
- 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
- 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.
- 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.
- 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
- 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.
- 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.
- 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.
- Sen, T., Mandal, S., Haldar, S., Chattopadhyay, K., and Patra, A., (2011) J. Phys. Chem. C, 115 (49), pp 24037–24044.
- 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
- 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.
- 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.
- 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.
- Chattopadhyay, K. & Frieden, C. (2006) Steady State and Time-resolved fluorescence studies of the intestinal fatty acid binding proteins, Proteins 63, 327-335.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- Chattopadhyay, K.; & Mazumdar, S. (2001) Direct electrochemistry of heme proteins: effect of electrode surface modification by neutral surfactants. Bioelectrochemistry 53, 17-24.
- Chattopadhyay, K.; & Mazumdar, S. (2000) Structural and conformational stability of horseradish peroxidase: effect of temperature and pH. Biochemistry 39, 263-270.
- Chattopadhyay, K.; &Mazumdar, S. (1999) Direct electrochemical oxidation of horseradish peroxidase: cyclic voltammetric and spectroelectrochemical studies. New J Chem 23, 137-139.