Explores protein folding, amino acids, RNA translation, and attractive forces, emphasizing the importance of native state conformation and compact structures.
Delves into protein folding principles, emphasizing sequence's role in determining structure and exploring thermodynamics and intermolecular interactions.
Explores proteinopathy mapping, connecting proteotoxicity to intrinsic functions of aggregation-prone proteins, with a focus on alpha-synuclein and Parkinson's Disease.
Explores the evolution and function of protein-repair machineries, emphasizing the role of ATP-fueled unfolding machines in preventing protein aggregation and promoting proper folding.
Explores the molecular chaperone action of small heat shock proteins in proteostasis, focusing on their interaction with misfolded proteins and amyloid fibrils.
Explores proteostasis regulation through chaperone interactions and post-translational modifications, revealing insights into protein quality control mechanisms.