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. Author manuscript; available in PMC: 2008 Dec 1.
Published in final edited form as: Nat Struct Mol Biol. 2008 May 30;15(6):591–597. doi: 10.1038/nsmb.1429

Figure 2.

Figure 2

CD spectra for the PT and MT-DT domains. (a) A typical CD spectrum of the PT showing the characteristic double minima of an α-helical protein. Inset, the thermal melt of the PT showing the cooperative melt typical of a folded protein. (b) CD spectra of the MT-DT as a monomer (red) or as an artificial dimer held together by a C-terminal disulfide bridge (blue). Inset, thermal melt curves showing that both constructs have a broad thermal unfolding transition as expected for a single α-helix. The similarity of the spectra and melt curves of the monomer and dimer indicates that no structural changes occur when the MT-DT is placed in conditions mimicking high concentrations. This indicates an inability of the MT-DT to dimerize.