Delves into protein folding principles, emphasizing sequence's role in determining structure and exploring thermodynamics and intermolecular interactions.
Explores the conformational and functional flexibility of Hsp70 molecular chaperones, focusing on folding intermediates and the Hsp70 functional cycle.
Explores protein structure determination using NMR and Cryo-EM techniques, covering chemical shifts, isotope labeling, NOE, and high-resolution imaging methods.
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.
