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. Author manuscript; available in PMC: 2010 Jan 16.
Published in final edited form as: J Mol Biol. 2008 Nov 1;385(2):628–641. doi: 10.1016/j.jmb.2008.10.046

Figure 6.

Figure 6

A comparison of thermally induced perturbations to Δ-domain secondary structure in vitro (top) and in situ (bottom). The models incorporate results of the Raman amide I band analyses and the sizes of the cooperative units (〈nc〉) determined from sedimentation and thermodynamic data (see text). A key feature is that at physiological temperature (37 °C) the structural organization of the in situ Δ-domain is greater than that of the in vitro Δ-domain. In particular, each chain of the in situ trimer retains full α-helicity, whereas the in vitro monomer is partially unfolded.