Explores translation, mutations, ribosome function, protein folding, and degradation processes, emphasizing the genetic code's role in protein synthesis.
Delves into protein aggregation mechanisms using C. elegans, covering misfolding, aggregation pathways, kinetics, chaperones, and stochastic nucleation.
Explores proteostasis regulation through chaperone interactions and post-translational modifications, revealing insights into protein quality control mechanisms.
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.
