Dr. Samrat Mukhopadhyay
Associate Professor, Biological Sciences & Chemical Sciences

Email:               mukhopadhyay(AT)iisermohali.ac.in

Phone:

Fax:                  +91 172 2240266

Personal Page:  The Mukhopadhyay Research Group

 

Research Area:

Intrinsically Disordered Proteins: Phase Transition, Misfolding, Aggregation, and Amyloid Formation.

 

Research Focus

Proteins are the workhorses of the living systems. Traditionally, protein function was thought to depend on a unique well-defined 3D structure that is encoded by the amino acid sequence. However, current investigations have revealed that a large fraction of the proteome consists of polypeptide segments that lack a well-defined structure under physiological conditions. They belong to a distinct class of proteins termed as intrinsically disordered proteins (IDPs) that challenge the tenets of the traditional structure-function paradigm. The intrinsic disorder in the proteins allows the complex organisms to carry out multiple functions from the same proteins by adopting different conformational states. However, the disorder-to-function relationship is poorly understood. Additionally, dysfunction of many IDPs is associated with a range of deadly diseases such as Alzheimer's disease, Parkinson's disease, Amyotrophic lateral sclerosis (ALS), frontotemporal dementias (FTDs) and cancers. The Mukhopadhyay lab utilizes a diverse range of approaches involving biophysics, biochemistry, chemical biology, cell and molecular biology, and advanced single-molecule and ultrafast spectroscopy to gain molecular insights into the conformational ensemble and dynamics, the protein hydration water, liquid-liquid phase separation, aggregation and amyloid formation from various IDPs containing low-complexity and prion-like domains. These studies are beginning to illuminate the unique molecular insights into the pivotal functional and pathological aspects of phase transition of IDPs.


Selected Publications

  • "Liquid-Liquid Phase Separation is Driven by Large-Scale Conformational Unwinding and Fluctuations of Intrinsically Disordered Protein Molecules" A. Majumdar, P. Dogra, S. Maity & S. Mukhopadhyay* J. Phys. Chem. Lett. 2019, 10, 3929−3936.
  • "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.
  • "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, 430, 2508-2520.
  • "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.
  • "Direct Observation of the Intrinsic Backbone Torsional Mobility of Disordered Proteins" N. Jain, D. Narang, K. Bhasne, V. Dalal, S. Arya, M. Bhattacharya, & S. Mukhopadhyay* Biophys. J. 2016, 111, 768-774.

    For a complete list of publications: Click here