Priya R. Banerjee, PhD

Assistant Professor

229 Fornczak Hall
(716) 645-3444
prbanerjea@gmail.com

Education

  • BS, University of Calcutta, India – 2005
  • MS, West Bengal University of Technology, India – 2007
  • PhD, University at Albany, SUNY – 2011
  • Postdoctoral Fellowship, The Scripps Research Institute – 2012-2017

Research Area

Specialties

Single-molecule biophysics, Intrinsically disordered proteins, Phase transition in proteins and nucleic Acids, Biomolecular engineering

Research Interests

Our lab focuses on understanding the physical principles of (non) folding and phase behavior of Intrinsically Disordered Proteins (IDPs) using sensitive, high-resolution single-molecule techniques. IDPs account for a significant portion of eukaryotic proteome(30 ‒ 50%). Although they challenge the classical protein structure-function paradigm, it is well established now that the disordered proteome performs important organizational, regulatory, and signaling functions in cells. Furthermore, IDPs are commonly associated with a broad repertoire of human diseases including neurodegeneration and cancer.

IDPs typically display a high degree of conformational plasticity and substantial structural heterogeneity, which severely limits the application of conventional ensemble methods of structural biology to elucidate their properties. Due to this, single-molecule methodologies are critical to study these dynamic biological systems by watching one molecule at a time. In our laboratory, we develop and apply advanced single-molecule fluorescence spectroscopy tools, in combination with fluorescence microscopy, complementary biophysical spectroscopy, and physical modeling. Additionally, we employ a diverse array of chemical and biological methods to interrogate our system of interest. Using this multidisciplinary strategy, we seek answers for how the specific amino acid sequence of IDPs control their individual interaction space in a multi-component system leading to (a) IDP coupled binding-folding behavior that encodes multi-functionality, and (b) IDP self-assembly into biomolecular condensates with tunable material properties. These answers will be critical in deciphering the molecular functions of the disordered proteome and mapping their operational pathways. By understanding IDP molecular properties, we can further explore plausible strategies for (i)ameliorating cellular homeostasis in disease states, and (ii) expanding the scope of bioinspired functional materials.

Awards and Honors

  • American Heart Association (AHA) Postdoctoral Fellow
  • Distinguished Doctoral Dissertation Award

Selected Publications

For a complete list of publications, please see Google Scholar.

  • Banerjee, P. R.*, Moosa M. M., Deniz, A. A.* 2016. Two-dimensional crowding uncovers a hidden conformation of α-synuclein. Angew Chem Int Ed Engl. 55(41):12789-92. (*Corresponding Authors). PubMed PMID: 27612332 
    News Release at the Scripps News and Views
  • Mitrea, D. M., Cika, J. A., Guy, C. S., Ban, D., Banerjee, P. R., Stanley, C. B., Nourse, A., Deniz, A. A., Kriwacki, R. W. 2016. NPM1 integrates within the nucleolus via multi-modal interactions with protein displaying R-rich linear motifs and rRNA. eLife;10.7554/eLife.13571. PubMed PMID: 26836305
  • Banerjee, P. R., Mitrea, D. M., Kriwacki, R. W., Deniz, A. A., 2016. Asymmetric Modulation of Protein Order-Disorder Transitions by Phosphorylation and Partner Binding. Angew Chem Int Ed Engl. 55(5):1675-9. PubMed PMID: 26679013
    News Release at the Scripps News and Views
    Featured in Faculty of 1000
  • Polinkovsky, M. E.*, Gambin, Y.*, Banerjee, P. R.*, Erickstad, M. J., Groisman, A., Deniz, A. A. 2014. Ultrafast cooling reveals microsecond-scale biomolecular dynamics. Nature Communications. 2014 Dec 17; 5:5737 (* Equal contribution first authors). PubMed PMID: 25517430
    News Release at the Scripps News and Views
    Highlighted in BioTechniques
  • Banerjee, P. R., Pande, A., Shekhtman, A., Pande, J. 2015. Molecular mechanism of the chaperone function of mini-α-crystallin, a 19-residue peptide of human α-crystallin. Biochemistry, 54 (2), 505–515. PubMed PMID: 25478825
    News Coverage in Chemical & Engineering News
  • Banerjee, P. R., Deniz, A. A. 2014. Shedding light on protein folding landscapes by single-molecule fluorescence. Chem. Soc. Rev. 43, 1172-1188. PubMed PMID: 24336839
  • Banerjee, P. R., Pande, A., Patrosz, J., Thurston, G. M., Pande, J. 2011. Cataract-associated mutant E107A of human gamma D-crystallin shows increased attraction to alpha-crystallin and enhanced light scattering.  Proc. Natl. Acad. Sci. (U.S.A) 108, 574-579. PubMed PMID: 21173272
    News Coverage in Chemical & Engineering News
    Commentary in Proc. Natl. Acad. Sci. (U.S.A)
  • Banerjee, P. R., Puttamadappa, S. S., Pande, A., Shekhtman, A., Pande, J. 2011. Increased hydrophobicity and decreased backbone flexibility explain the lower solubility of a cataract-linked mutant of gammaD-crystallin. J. Mol. Biol. 412, 647-659. PubMed PMID: 21827768