Our research interests are in the area of theoretical/computational biophysics and polymer physics. Proteins synthesized in the cell generally fold into specific 3-dimensional structures to perform their functions. Due to undue stresses on the cell, misfolding and aggregation of proteins can occur, which lead to pathological diseases. Our research is geared towards understanding the basic principles involved in protein folding/aggregation, DNA-protein interactions and DNA condensation. Depending on the system of interest we use and develop atomistic, coarse-grained and continuum based protein-DNA models, and appropriate theoretical/computational techniques to gain insight into the relevant physics of the phenomenon.
- A. Panjal and G. Reddy, “Osmolyte effects on the growth of amyloid fibrils”, J. Phys. Chem. B, 120 (2016) 10979.
- H. Maity and G. Reddy, “Folding of Protein L with implications for collapse in the denatured state ensemble”, J. Am. Chem. Soc., 138 (2016) 2609.
- G. Reddy and D. Thirumalai, Dissecting Ubiquitin folding using the self-organized polymer model, J. Phys. Chem. B 119 (2015) 11358.
- G. Reddy, Z.X. Liu and D. Thirumalai, Denaturant-dependent folding of GFP, Proc. Natl. Acad. Sci. 109 (2012) 17832.
- Z.X. Liu, G. Reddy, E.P. O’Brien and D. Thirumalai, Collapse kinetics and Chevron plots from simulations of denaturant-dependent folding of globular proteins, Proc. Natl. Acad. Sci. 108 (2011) 7787.
- G. Reddy, J.E. Straub and D. Thirumalai, Dry amyloid fibril assembly in a yeast prion peptide is mediated by long-lived structures containing water wires, Proc. Natl. Acad. Sci. 107 (2010) 21459.