The effect of nucleotide exchange factor on its partner, the E. coli Hsp 70 DnaK, is based on conformational changes
Maria-Agustina Rossi, UMAss Amherst (USA)
70-kDa heat shock proteins (Hsp70s) assist in protein folding and rescue proteins from aggregation. The Hsp70 allosteric cycle is ATP-dependent, and is modulated by co-chaperones; nucleotide exchange factors (NEFs) bind to Hsp70 and promote the replacement of ADP with ATP. Here, we aim to understand the structural basis of the interaction and how the NEF promotes nucleotide exchange. To answer these questions we applied diverse techniques that led us to the idea that GrpE promotes conformational changes on the NBD to achive this goal.
Structural insights into Amelotin oligomerization by pressure-jump NMR spectroscopy
Sai Chiliveri, National Institutes of Health (USA)
Amelotin plays a crucial role in the hydroxyapatite mineralization of dental enamel. Due to their dynamic and heterogeneous nature, large oligomeric species formed by Amelotin are not amenable to structural studies at the residue-specific level. Here, we present new pressure-jump NMR methods for probing the structure of oligomeric species. Secondary and tertiary structure information on the oligomers obtained from 13C chemical shifts and 1H-1H nuclear Overhauser enhancements (NOE) will be demonstrated.
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