Figure 7From: Solution structure of the parvulin-type PPIase domain of Staphylococcus aureus PrsA – Implications for the catalytic mechanism of parvulinsDynamical features of S. aureus PrsA-PPIase. Generalized order parameters (S2) for backbone amides were calculated using ModelFree formalism from 15N R1 and R2 relaxation rates and 1H-15N heteronuclear NOEs. (A) Generalized order parameter (S2) as function of residue sequence for PrsA-PPIase (dark grey) and for PrsA-PPIase + Suc-AEPF-p NA (light grey). (B) S2 changes induced upon Suc-AEPF-p NA peptide addition averaged over three consecutive residues. (C) Backbone amide proton exchange rates as function of residue sequence for PrsA-PPIase (box) and PrsA-PPIase + Suc-AEPF-p NA (cross). Position of the secondary structure elements in the sequence is shown on the top panel: green arrow – β-strand; red bar – α-helix.Back to article page