Dr. Krishnananda Chattopadhyay
Scientist E1
Indian Institute of Chemical Biology
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(at)iicb.res.in
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Current
Research Interest
- Fluorescence
Correlation Spectroscopy and Protein Folding
- Protein stability, mis-folding and aggregation
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List
of important Publications:
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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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