Molecular Simulations of Heat Shock Proteins
The three-dimensional structure of proteins is essential to their proper functioning. Chaperone proteins help misfolded proteins unfold and refold to their correct conformations and are critical for the maintenance of proteome integrity. These are highly conserved across almost all branches of life. Our particular interest in chaperone proteins is that cancer cells rely on these for survival and hence, these may constitute an attractive new therapeutic target. Our goal is to uncover the working of the mammalian heat shock protein 70 through molecular simulations, and to investigate potential inhibitors. The project will involve the study of the protein through all atom molecular simulations, docking and other computational methods to interrogate chaperone function and discover modulators.
Skills Required: An interest in modelling and simulations is required. Coding skills in any language is desirable .