Figure 6: Structural validation of protein switches. | Nature Communications

Figure 6: Structural validation of protein switches.

From: Design of protein switches based on an ensemble model of allostery

Figure 6

(a) Percentage of residues mapped from the 15N-TROSY-HSQC spectra of c4 and c4-3G onto the spectra of MBP37 and BLA38. (b) An overlay of the c4 (black) and c4-3G (red) 15N-TROSY-HSQC spectra at 37 °C in the absence of maltose. The labels represent the peripheral peaks in the c4 spectrum that are not present in the c4-3G spectrum. These missing peaks were manually examined and attributed to residues of MBP (underlined italic) and BLA (regular text) domains. The central region of the spectra that was excluded from examination is shaded in grey. The corresponding missing residues are (c) mapped onto the MBP and BLA domain of the model structure of c4-3G and highlighted in red. Green indicates residues with peripheral resonances present in the spectra of both c4 and c4-3G.

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