Fig. 7: Sb4 is an equilibrium mixture of S- and B-states.
From: Design and characterization of a protein fold switching network
a Two-dimensional 1H–15N HSQC spectra of Sb4 (left), B4 (center), and Sb3 (right) at 25 °C. In the Sb4 spectrum, backbone amide resonance assignments are shown for the S-state (blue) and the B-state (red). b Confidence levels of ordered secondary structure regions for the S-state of Sb4 at 30 °C (red) and for Sb3 at 25 °C (gray) from chemical shifts using TALOS-N. The secondary structure elements of Sb3, determined from the three-dimensional structure, are shown above the plot. c Summary of long-range backbone NOEs from 3D 15N-NOESY data for Sb3 at 25 °C (black) and the S-state of Sb4 at 30 °C (red). d Gly41 region of the 300 ms ZZ-exchange spectrum for Sb4 at 25 °C, showing exchange peaks between the S- and B-states.
