Fig. 3
Peptides protected by the E9 A20 C-ter interaction determined by H/D exchange MS. a Peptides from E9, identified by LC-MS/MS, are represented as bars above the primary sequence. The secondary structure, derived from the crystal structure, is shown underneath the sequence (in gray residues not seen in the structure). The level of protection of individual peptides, as determined by comparing the % D incorporation for free E9 with the one for E9 bound to A20 C-ter, is color coded according to the scale bar. Highly protected areas are shown in red, whereas peptides becoming more exposed upon complex formation are shown in blue. The highly protected region involves the α-helix of insert 3 (residues 577–590). b H/D exchange results are mapped onto the crystal structure of E9. Protected residues are color coded as in a
