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 beta-hairpins in polyglutamine protein aggregation, focusing on Huntington's disease and the molecular mechanisms behind toxic fibril formation.
Delves into protein aggregation mechanisms using C. elegans, covering misfolding, aggregation pathways, kinetics, chaperones, and stochastic nucleation.
Explores the conformational and functional flexibility of Hsp70 molecular chaperones, focusing on folding intermediates and the Hsp70 functional cycle.
Explores translation, mutations, ribosome function, protein folding, and degradation processes, emphasizing the genetic code's role in protein synthesis.
