Arlind Kacirani
Arlind Kacirani ‘26
Home Department: Chemical and Environmental Engineering (Haji-Akbari Lab)
Research Project: The effect of thermodynamic perturbations in folding of human γD-crystallin using replica exchange molecular dynamics simulations.
Crystallins are an important class of lens proteins that are responsible for maintaining the high refractive index of the lens. However, packed in a very crowded environment, mutations and physicochemical perturbations lead to the misfolding and the subsequent accumulation of heterogeneous and high molecular weight aggregates whose light scattering is the molecular cause of cataracts. In our group we are looking at the effect of thermodynamic variables like T, P and solvent composition on the intra- and intermolecular interactions in human γD-crystallin using MD simulations and enhanced sampling methods.
Relevant Publications
Structural features highlight the effect of pressure on conformational dynamics: N-td aromatic contacts (left), protein end-to-end distance (middle), hydration status of interdomain interface (right)