Figure 4 | Scientific Reports

Figure 4

From: Ionic strength-dependent conformations of a ubiquitin-like small archaeal modifier protein (SAMP2) from Haloferax volcanii

Figure 4

15N-HSQC spectra and solution structure of SAMP2 in different concentrations.

(a) The 1H-15N-HSQC spectra of SAMP2 in different concentrations of NaCl. The salt concentrations are 0 M, 0.1 M, 0.5 M and 1 M of NaCl, respectively. Note that all the weakened and disappeared resonances of SAMP2 belong to the disordered state and are distributed between 8.0–8.7 ppm of HN. (b) Solution structure of SAMP2 under high ionic condition (1 M NaCl). Left: Ribbon structure of a representative conformer of SAMP2 with the secondary structure elements highlighted. Right: Backbone superposition of 20 selected conformers with the lowest energy from the final CNS calculation. (c) Structural comparison of SAMP2 under low and high ionic conditions. Blue: structure in low salt. Green: structure in high salt.

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