Figure 2: NMR spectra of substrate-free WT AKe, M1 and M2 mutants.
From: Overlap between folding and functional energy landscapes for adenylate kinase conformational change
In (a) and (b), WT AKe is shown with blue contouring and the two mutants are contoured red. (a) Superimposition of 1H-15N HSQC spectra of WT AKe and M1 acquired at 25 °C. (b) Superimposition of 1H-15N HSQC spectra of WT AKe and M2 acquired at 25 °C. Selected resonances in the INSERT segment of the ATPlid that are missing in the M2 mutant are indicated. (c) Superimposition of 1H-15N HSQC spectra of M2 acquired at 25 °C (red contours) and 15 °C (blue contours). Selected resonances (same set as in b) corresponding to residues in the INSERT segment in ATPlid are indicated.
