IISER Mohali, Knowledge city, Sector 81, SAS Nagar, Manauli PO 140306

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

Email mukhopadhyay(AT)iisermohali.ac.in
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
    • "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.
    • "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" 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


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