Current team

Arshad A works primarily on tau protein with experience on various tau constructs which include htau40 and its microtubule binding repeats. His work broadly involves on the monomeric behavior of Tau constructs, their phase separation behavior and seeding properties studied through various NMR relaxation techniques and other conventional biophysical methods.

Safwa T K works on TIA-1, the RNA binding protein responsible for the formation of stress granules. Safwa’s work focuses on the droplet forming behavior of various TIA-1 constructs with tau protein and their response to changes in environmental conditions such as salt, pH etc., using biophysical techniques such as NMR, fluorescence microscopy, etc.

Allwin works on understanding the conformational properties of Tau protein through mutational studies using molecular dynamics simulations and experimentally by monitoring aggregation properties of mutants. 

Ann works on to explore the interactions present between functional prion CPEB3 against pathological tau protein which are both found in the membrane rich region of the neuronal cells. Currently, Ann works on the interactions between various motifs of PRD1 with K18 tau construct. 

Faina primarily studies CPEB3, a functional prion protein responsible for long-term potentiation in mammals. Currently, Faina focuses on the prion domain (PRD2) of both human and mouse CPEB3 to compare the phase separation properties of both the orthologs. Faina predominantly uses 3D NMR techniques for structural analysis and other biophysical techniques for probing aggregation.