Figure 1: The cold and hot denatured states of frataxin are structurally different.
From: Towards a structural biology of the hydrophobic effect in protein folding
(a) Structure of the native state of frataxin. (b) Free energy surface of the cold denatured state (CDS) determined at 272 K as a function of the sketch-map63 collective variables that describe the conformational features of the ensembles (see Methods). Nine microstates are shown representing the local and global minima. These microstates comprise >90% of the total population. (c) Free energy surface of the hot denatured state (HDS) determined at 323 K as a function of the same two collective variables. Sixteen microstates are shown representing the local and global minima. These microstates comprise >90% of the total population (see Methods). (d,e) Secondary structure populations of the CDS (d) and HDS (e). α-Helices are represented in blue, β-strands in red and polyproline II in green; free energies are given in kJ/mol.
