Explores the molecular chaperone action of small heat shock proteins in proteostasis, focusing on their interaction with misfolded proteins and amyloid fibrils.
Explores proteinopathy mapping, connecting proteotoxicity to intrinsic functions of aggregation-prone proteins, with a focus on alpha-synuclein and Parkinson's Disease.
Explores the selective promiscuity in binding of the E. coli Hsp70 chaperone to unfolded or misfolded protein substrates, examining its implications in protein folding mechanisms.
Explores protein folding, amino acids, RNA translation, and attractive forces, emphasizing the importance of native state conformation and compact structures.
