An update on the biophysical character of the human eukaryotic elongation factor 1 beta: Perspectives from interaction with elongation factor 1 gamma.

The β-subunit of the human eukaryotic elongation factor 1 complex (heEF1β) plays a central role in the elongation step in eukaryotic protein biosynthesis, which essentially involves interaction with the α- and γ-subunits (eEF1γ). To biophysically characterize heEF1β, we constructed 3 Escherichia coli expression vector systems for recombinant expression of the full length (FL-heEF1β), N-terminus (NT-heEF1β), and the C-terminus (CT-heEF1β) regions of the protein. Our results suggest that heEF1β is predominantly alpha-helical and possesses an accessible hydrophobic cavity in the CT-heEF1β.