Explores translation, mutations, ribosome function, protein folding, and degradation processes, emphasizing the genetic code's role in protein synthesis.
Covers the analysis of post-translational modifications using mass spectrometry, focusing on techniques, challenges, and the significance of phosphoproteomics.
Explores post-translational modifications and folding processes in the endoplasmic reticulum, using examples like the influenza virus and protein misfolding diseases.
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 the molecular chaperone action of small heat shock proteins in proteostasis, focusing on their interaction with misfolded proteins and amyloid fibrils.
