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. 2018 Mar 10;46(8):4044–4053. doi: 10.1093/nar/gky176

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© The Author(s) 2018. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 1. — Disorder and collapse. (A) Far-UV CD spectra of CytR (blue) and PurR (red) at 298 K in mean residue ellipticity units of deg. cm² dmol⁻¹. (B) Changes in the hydrodynamic radius (R_h) of CytR with temperature extracted from dynamic light scattering measurements. The curves are shown to guide the eye. Shaded regions in pink and blue represent the hydrodynamic radius of disordered and ordered proteins, respectively, from size-scaling expectations (44). The green triangle represents the R_h of CytR from the DNA-bound structure at 308 K calculated using HYDROPRO (45).