Fig. 3: Structure and dynamics of A1 and Sa1.
From: Design and characterization of a protein fold switching network
a Sequence alignment of A1 and Sa1, which are 100% identical over the 56 amino acid A-region. b Overlaid two-dimensional 1H-15N HSQC spectra of Sa1 (black) and A1 (red) with backbone amide assignments. Spectra were recorded at 25 and 5 °C, respectively. c Ensemble of 10 lowest energy CS-Rosetta structures for A1 (left panel). Superposition of the A1 structure (green) with the parent GA fold (orange) (right panel). d Ensemble of 10 lowest energy CS-Rosetta structures for Sa1 (left panel). Superposition of Sa1 (green) with the parent S6 fold (orange) (right panel). e Backbone dynamics in designed proteins. Plot of {1H}-15N steady state heteronuclear NOE values at 600 MHz versus residue for A1 (red) and for Sa1 (black). Each set of heteronuclear NOEs was obtained from a single experiment. Errors were estimated based on the measured background noise level.
