Dr. Samrat Mukhopadhyay

   Asssociate Professor (Biology & Chemistry)
   Knowledge city, Sector 81, SAS Nagar,
   Manauli PO 140306

   Email: mukhopadhyay[at]
   Tele: +91-172-224-0209
   Telefax: +91-172-224-0266

Research Area: Intrinsically Disordered Proteins; Protein Misfolding & Aggregation; Chemical Biophysics of Amyloids; Single-Molecule, Ultrafast & Nanoscale Biophysics

Proteins are the workhorses of the living systems. For carrying out specific functions, proteins have to fold up correctly. Incorrect folding or protein misfolding can lead to amyloid aggregation and is implicated in a number of neurological disorders such as Alzheimer's, Parkinson and prion diseases. The molecular mechanisms of protein folding, misfolding, aggregation and amyloid fibril formation are poorly understood. Our laboratory is actively involved in unraveling the molecular mechanism of aggregation of a diverse class of proteins using a diverse array of biophysical techniques, combined with modern cellular and molecular biology tools. My lab is now embarking upon a very unique and novel direction. Many of these amyloid forming proteins are intrinsically disordered proteins (IDPs) that confront the traditional sequence-structure-function paradigm. IDPs lack the ability to undergo autonomous folding, exist as dynamic ensembles and showcase the importance of conformational plasticity and heterogeneity in the protein function We are also investigating the role of water in the disorder-to-order amyloid transition of IDPs. Our interdisciplinary efforts involve tools and concepts of biology, chemistry and physics.

Selected Publications

  • "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.
  • "Direct Observation of the Intrinsic Backbone Torsional Mobility of Disordered Proteins by Fluorescence Depolarization Kinetics" N. Jain, D. Narang, K. Bhasne, V. Dalal, S. Arya, M. Bhattacharya, & S. Mukhopadhyay Biophys. J. 2016 111, 768-774.
  • "Confined Water in Amyloid-Competent Oligomers of the Prion Protein" V. Dalal, S. Arya, & S. Mukhopadhyay Chem PhysChem 2016 17, 2804-2807.
  • "Characterization of Salt-Induced Oligomerization of Human Beta2-Microglobulin at Low pH" D. Narang, A. Singh, H.M. Swasthi & S. Mukhopadhyay J. Phys. Chem. B. 2016 120, 7815-7823.
  • "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, 7505−7513.

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