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Structural Biology & Bio-Informatics Division
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Dr. Krishnananda Chattopadhyay
Senior 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
Contact – krish@iicb.res.in |
Current Research Interest
- Fluorescence Correlation Spectroscopy and Protein Folding
- Protein Stability and Aggregation
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List of important Publications:
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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
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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.
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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
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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.
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Chattopadhyay, K. & Frieden, C. (2006) Steady State and Time-resolved fluorescence studies of the intestinal fatty acid binding proteins, Proteins 63, 327-335.
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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.
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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.
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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.
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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.
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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.
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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.
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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.
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Chattopadhyay, K.; & Mazumdar, S. (2001) Direct electrochemistry of heme proteins: effect of electrode surface modification by neutral surfactants. Bioelectrochemistry 53, 17-24.
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Chattopadhyay, K.; & Mazumdar, S. (2000) Structural and conformational stability of horseradish peroxidase: effect of temperature and pH. Biochemistry 39, 263-270.
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Chattopadhyay, K.; &Mazumdar, S. (1999) Direct electrochemical oxidation of horseradish peroxidase: cyclic voltammetric and spectroelectrochemical studies. New J Chem 23, 137-139
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| Updated on 26th August' 2011 |
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