C-Terminal Amino Acids Are Essential for Human Heat Shock Protein 70 Dimerization

Marcion G, et al., pp 61-72, Cell Stress and Chaperones, 2015

This article describes the heterologous expression and purification of soluble, full length, non-tagged human inducible heat shock protein 70 (hHsp70). Homodimerizing behavior of hHsp70 and important C-terminal residues of interest were demonstrated using multi angle light scattering and Bio-Layer Interferometry (BLI). A Pall ForteBio Octet RED system equipped with Streptavidin Biosensor probes was used to capture biotinylated Hsp70 or DnaK and then dipped into wells containing a serial dilution of Hsp70 and DnaK. In another experiment, the dimerized species (Hsp70 or DnaK) were tested for binding with a biotinylated peptide-aptamer ligand A17.

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