Additional file 2: Figure S2. of Prokaryotic ubiquitin-like protein remains intrinsically disordered when covalently attached to proteasomal target proteins
Secondary shifts of Mtb Pup ~ Mtb FabD and Mtb Pup ~ lysine. Chemical shifts of the native protein ( Mtb Pup ~ Lys in red, Mtb Pup ~ Mtb FabD-3KR in green) minus shifts for Mtb Pup ~ Mtb PanB unfolded in Urea (data from [3]). The region with helical propensity in free Mtb Pup is indicated in grey. (PNG 213 kb
