Welcome to the Homepage of Samrat Mukhopadhyay

Dr. Samrat Mukhopadhyay, Ph.D.                           

Associate Professor,
Centre for Protein Science, Design and Engineering
Department of Biological Sciences & Department of Chemical Sciences,  
Indian Institute of Science Education and Research (IISER), Mohali. 
Knowledge City, Sector 81, S.A.S. Nagar, Mohali-140306, Punjab, India.

We had an exciting International Conference on Intrinsically Disordered Proteins: Forms, Functions and Diseases (IDP 2017) at IISER Mohali December 9-12, 2017. The final program is here 

Guest Editor, Special Issue on Intrinsically Disordered Proteins in BBA Proteins and Proteomics: 

Please note that we do not update our website frequently. Our recent news can be found on our twitter.

Research interests:
Intrinsically Disordered Proteins; Protein Misfolding & AggregationAmyloid Biology;  Single-Molecule, Ultrafast & Nanoscale Biophysics; Chemical Biophysics


List of publications: (Total citations: > 2000   h-index = 18)
Open Researcher & Contributor ID (ORCID) 0000-0003-1242-9958

Read my book-review on "Madness and Memory: The Discovery of Prions – A New Biological Principle of Disease" by Stanley Prusiner. 

Read our new papers in Journal of Molecular Biology, Biophysical Journl and Biochemistry: 

39.  "Human Fibrinogen Inhibits Amyloid Assembly of Biofilm-Forming CsgA" Hema M. Swasthi, Karishma Bhasne, Sayanta Mahapatra, and Samrat Mukhopadhyay Biochemistry 2018.

38. "Femtosecond Hydration Map of Intrinsically Disordered α-Synuclein" S. Arya, A. Singh, K. Bhasne, P. Dogra, A. Datta,* P. Das,* & S. Mukhopadhyay* Biophys. J. 2018,  114, 2540–2551.

37. "Synergistic Amyloid Switch Triggered by Early Heterotypic Oligomerization of Intrinsically Disordered α-Synuclein and Tau" K. Bhasne, S. Sebastian, N. Jain, & S. Mukhopadhyay* J. Mol. Biol. 2018 
Featured in Faculty of 1000

36. "Electrostatic lipid-protein interactions sequester the curli amyloid fold on the lipopolysaccharide membrane surface" H.M. Swasthi & S. Mukhopadhyay* J. Biol. Chem. 2017, 292, 19861-19872.

Featured in special virtual issue: http://www.jbc.org/site/vi/amyloids/

35. "Site-Specific Fluorescence Depolarization Kinetics Distinguishes the Amyloid Folds Responsible for Distinct Yeast Prion Strains" D. Narang, H.M. Swasthi, S. Mahapatra & S. Mukhopadhyay* J. Phys. Chem. B. 2017, 121, 8447-8453.

34. "Detergent-induced Aggregation of an Amyloidogenic Intrinsically Disordered Protein" S. Arya, P. Dogra, N. Jain & S. Mukhopadhyay* J. Chem. Sci. 2017, 129, 1817–1827.

33. "pH-Responsive Mechanistic Switch Regulates the Formation of Dendritic and Fibrillar Nanostructures of a Functional Amyloid" P. Dogra, M. Bhattacharya & S. Mukhopadhyay*  J. Phys. Chem. B2017121, 412-419.

32. "Water Rearrangements upon Disorder-to-Order Amyloid Transition" S. Arya, A. K. Singh, T. Khan, M. Bhattacharya, A. Datta,* & S. Mukhopadhyay* J. Phys. Chem. Lett. 2016, 7, 4105−4110. 

Click below to play and listen to the presentation! 

31. "Direct Observation of the Intrinsic Backbone Torsional Mobility of Disordered Proteins" N. Jain..... S. Mukhopadhyay Biophys. J.  2016, 111, 768-774.  
Featured in Faculty of 1000

30. "Characterization of Salt-Induced Oligomerization of Human β2-Microglobulin at Low pHD. Narang, A. Singh, H.M. Swasthi & S. Mukhopadhyay  J. Phys. Chem. B. 2016 (in press). 

29.  "Confined Water in Amyloid-competent Oligomers of the Prion Protein" V. Dalal, S. Arya & S. Mukhopadhyay  ChemPhysChem  2016 (accepted). http://onlinelibrary.wiley.com/doi/10.1002/cphc.201600440/full  

28. "Stepwise unfolding of human β2‑microglobulin into a disordered amyloidogenic precursor at low pH" D. Narang, A. Singh & S. Mukhopadhyay  Eur. Biophys. J. 2016

27. "Conformational Switching and Nanoscale Assembly of Human Prion Protein into Polymorphic Amyloids via Structurally Labile Oligomers"  V. Dalal, S. Arya, M. Bhattacharya & S. Mukhopadhyay Biochemistry, 2015, 54, 7505-13.
27. "Appearance of Annular Ring-like Intermediates during Amyloid Fibril Formation from Human Serum Albumin" S. Arya, A. Kumari, V. Dalal, M. hattacharya & S. Mukhopadhyay  Phys. Chem. Chem. Phys. 2015, 17, 22862-22871

26. "Ordered Water within the Collapsed Globules of an Amyloidogenic Intrinsically Disordered Protein" S. Arya & S. Mukhopadhyay  J. Phys. Chem. B. 2014, 118, 9191–9198.

25. "Nanophotonics of Protein Amyloids" M. Bhattacharya & S. Mukhopadhyay  Nanophotonics 2014, 3, 51-59.
24. "Structural and Dynamical Insights into the Membrane-bound α-Synuclein" N. Jain, K. Bhasne, M. Hemaswasthi & S. Mukhopadhyay  PLoS ONE 2013, 8(12):e83752.

23.   "Nanoscale Optical Imaging of Amyloid Fibrils" V. Dalal, S. Arya & S. Mukhopadhyay in 'Bionanoimaging: Protein Misfolding & Aggregation' (Elsevier 2013  Editors: Y. Lyubchenko & V. Uversky).
22.  "Dynamics and Dimension of an Amyloidogenic Disordered State of Human β2-Microglobulin" D. Narang, P.K. Sharma & S. Mukhopadhyay. Eur. Biophys. J. 2013, 42, 767-76. 
21. "Nanoscopic Amyloid Pores Formed via Stepwise Protein Assembly" M. Bhattacharya, N. Jain, P. Dogra, S. Samai & S. Mukhopadhyay. J. Phys. Chem. Lett. 2013, 4, 480-85.  http://dx.doi.org/10.1021/jz3019786
20. "Nanoscale Fluorescence Imaging of Single Amyloid Fibrils" V. Dalal, M. Bhattacharya, D. Narang, P.K. Sharma & S. Mukhopadhyay. J. Phys. Chem. Lett. 2012, 3, 1783-1787 (DOI: 10.1021/jz300687f; http://pubs.acs.org/doi/abs/10.1021/jz300687f)


19.  "Conserved features of intermediates in amyloid assembly determine their benign or toxic states" R. Krishnan, J.L. Goodman, S. Mukhopadhyay, C.D. Pacheco, E.A. Lemke, A.A. Deniz & S. Lindquist. Proc. Natl. Acad. Sci. U.S.A. 2012. doi:10.1073/pnas.1209527109.
 These authors contributed equally to this work.
18. "Structural and Dynmical Insights into the Molten-Globule form of Ovalbumin" M. Bhattacharya and S. Mukhopadhyay.     J. Phys. Chem. B. 2012, 116, 520-531. http://pubs.acs.org/doi/abs/10.1021/jp208416d
17.  "Chain Collapse of an Amyloidogenic Intrinsically Disordered Protein" N. Jain, M. Bhattacharya and S. Mukhopadhyay. Biophys. J.  2011, 101, 1720-1729.  http://www.cell.com/biophysj/retrieve/pii/S0006349511009702 
Featured in Faculty of 1000   http://f1000.com/13409028

16. "Insights into the Mechanism of Aggregation and Fibril Formation from Bovine Serum Albumin" M. Bhattacharya, N. Jain and S. Mukhopadhyay. J. Phys. Chem. B. 2011, 115, 41954205.  http://pubs.acs.org/doi/abs/10.1021/jp111528c
15. "Studying Protein Misfolding and Aggregation using Fluorescence Spectroscopy" M. Bhattacharya and S.Mukhopadhyay* Reviews in Fluorescence 2011 (Invited review and will be published soon).
14. "pH-induced Conformational Isomerization of Bovine Serum Albumin Studied by Extrinsic and Intrinsic Protein Fluorescence" M. Bhattacharya, N. Jain, K. Bhasne, V. Kumari and S. Mukhopadhyay Journal of Fluorescence  2011, 21, 1083-1090. 

13. "Kinetics of Surfactant-induced Aggregation of Lysozyme Studied by Fluorescence Spectroscopy" N. Jain, M. Bhattacharya and S. Mukhopadhyay. Journal of Fluorescence  2011, 21, 615-625. 

12. "Direct and Selective Elimination of Specific Prions and Amyloids by 4,5-Dianilinophthalimide and Analogs" H. Wang, M.L. Duennwald, B.E. Roberts, L.M. Rozeboom, Y.L. Zhang, A.D. Steele, R. Krishnan, L.J. Su, D. Griffin, S. Mukhopadhyay, E.J. Hennessy, P. Weigele, B.J. Blanchard, J. King, A.A. Deniz, S.L. Buchwald, V.M. Ingram, S. Lindquist and J. Shorter. Proc. Natl. Acad. Sci. U.S.A. 2008, 105, 7159-7164. http://www.pnas.org/cgi/reprint/105/20/7159 
11. "Single-Molecule Biophysics: At the Interface of Biology, Physics and Chemistry" A.A. Deniz, S. Mukhopadhyay and E.A. Lemke J. R. Soc. Interface 2008, 5, 15-45. http://www.journals.royalsoc.ac.uk/content/0x116338np247206/fulltext.pdf
Among the most read articles at JRSI

10. "A natively unfolded yeast prion monomer adopts an ensemble of collapsed and rapidly fluctuating structures" S. Mukhopadhyay, R. Krishnan, E. A. Lemke, S. Lindquist and A.A. Deniz. Proc. Natl. Acad. Sci. U.S.A. 2007, 104, 2649-2654. http://www.pnas.org/cgi/reprint/104/8/2649.pdf
(Featured in Scripps News & Views and cited over 120 times)

9. "Biomolecular structure and dynamics using fluorescence from single diffusing molecules" S. Mukhopadhyay and A.A. Deniz. J. Fluorescence 2007, 17, 775-783. http://www.springerlink.com/content/f251382u545551v2/fulltext.pdf

8. "Characterization of amyloid fibril formation by mapping residue-specific fluorescence dynamics" S. Mukhopadhyay, P. Nayak, J. B. Udgaonkar and G. Krishnamoorthy. J. Mol. Biol. 2006, 358, 935-942. http://dx.doi.org/10.1016/j.jmb.2006.02.006

7. "Advances in Molecular Hydrogels" S. Bhattacharya, U. Maitra, S. Mukhopadhyay, A. Srivastava in "Molecular Gels" 2006. P. Terech, R.G. Weiss (Eds.) Kluwer Academic Publishers, The Netherlands. http://www.springerlink.com/content/w3282465784v7036/
6. "Structure and Dynamics of a Molecular Hydrogel" S. Mukhopadhyay, Uday Maitra, Ira, G. Krishnamoorthy, J. Scmidt and Y. Talmon  J. Am. Chem. Soc. 2004, 126, 15905-15914. http://pubs.acs.org/cgi-bin/article.cgi/jacsat/2004/126/i48/pdf/ja046788t.pdf

5. "Facile Synthesis, Aggregation Behavior, and Cholesterol Solubilization of Avicholic Acid" S. Mukhopadhyay and U. Maitra. Organic Lett. 2004, 6, 31-34. http://pubs.acs.org/cgi-bin/article.cgi/orlef7/2004/6/i01/pdf/ol036073f.pdf

4. "Chemistry and Biology of Bile Acids: A Review" S. Mukhopadhyay and U. Maitra Curr. Sci. 2004, 87, 1666-1683. http://www.ias.ac.in/currsci/dec252004/1666.pdf

3. "Dynamics of Bound Dyes in a Non-polymeric Aqueous Gel Derived from a Tripodal Bile Salt" S. Mukhopadhyay, Ira, G. Krishnamoorthy and U. Maitra.  J. Phys. Chem. B. 2003, 107, 2189-2192. http://pubs.acs.org/cgi-bin/article.cgi/jpcbfk/2003/107/i10/pdf/jp027079+.pdf

2. "Hydrogel Route to Nanotubes of Metal Oxides and Sulfates" G. Gundiah, S. Mukhopadhyay, U.G. Tumkurkar, A. Govindaraj, U. Maitra and C.N.R. Rao.  J. Mater. Chem. 2003, 13, 2118-2122. http://www.rsc.org/Publishing/Journals/JM/article.asp?doi=b304007k


"Hydrophobic Pockets in a Non-polymeric Aqueous Gel: Observation of such a Gelation Process by Color Change" U. Maitra, S. Mukhopadhyay, A. Sarkar, P. Rao and S.S. Indi.  Angew. Chem. Int. Ed. 2001, 40, 2281-2283. (Cited  over 120 times).