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.
- B. Mondal and G. Reddy. A transient intermediate populated in prion folding leads to domain swapping. Biochemistry. 2019, DOI: 10.1021/acs.biochem.9b00621.
- H. Maity, A. Muttathukattil and G. Reddy. Salt effects on protein folding thermodynamics. J. Phys. Chem. Lett. 2018, 9, 5063.
- H. Maity and G. Reddy. Thermodynamics and kinetics of single chain Monellin folding with structural insights into specific collapse in the denatured state ensemble. J. Mol. Biol. 2018, 430, 465.
- Dey and G. Reddy. Toroidal condensates by semiflexible polymer chains: Insights into nucleation, growth and packing defects. J. Phys. Chem. B 2017, 121, 9291.
- Muttathukattil and G. Reddy. Osmolyte effects on the growth of amyloid fibrils. J. Phys. Chem. B 2016, 120, 10979.
- Maity and G. Reddy. Folding of Protein L with implications for collapse in the denatured state ensemble. J. Am. Chem. Soc. 2016, 138, 2609.