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. Author manuscript; available in PMC: 2019 Jul 3.
Published in final edited form as: Structure. 2018 May 17;26(7):936–947.e3. doi: 10.1016/j.str.2018.04.008

Figure 3. Thermophilic Decoration Protein Has Enhanced Stability Compared with Mesophilic Homologs.

Figure 3.

(A) P74–26 gp87 forms a stable trimer in solution as determined by size-exclusion chromatography-multi-angle light scattering. Predicted molecular mass, 49 kDa; measured molecular mass, 52 kDa.

(B) Representative equilibrium fraction unfolding curve of P74–26 gp87 at 5 μM shows a steep unfolding transition from 3 to 4 M GdnHCl; excitation, 295 nm; emission, 325 nm. The solid line represents the global fit to a model of trimer to three unfolded monomers. Blue arrow indicates the comparable transition midpoint of λ gpD unfolding.