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. Author manuscript; available in PMC: 2013 Mar 1.
Published in final edited form as: Proteins. 2011 Dec 21;80(3):920–934. doi: 10.1002/prot.23249

Figure 3.

Figure 3

(a) Figure 2 from Matsumura et al, used by permission, showing the changes in melting temperature for reduced versus oxidized disulfide mutants of T4 lysozyme. (b) Changes in equilibrium unfolding point, as ω value, in GeoFold simulations. Mutants 127-154 and 90-122 unfold at the same w at WT*. (c-d) Age plot for unfolding pathway of (c) wild type T4 lysozyme, or reduced, or 127-154 or 90-122 mutants, and (d) oxidized 21-142 or 9-164 mutants, with contacts colored red to blue according to unfolding order. Upper inset in (c-d): first unfolding step, a pivot move in (c), a hinge move in (d). Lower inset: ribbon drawing showing how the structure is divided in the first unfolding step by (c) the pivot move p, and (d) the hinge move h.