Cold residue studies

Fig. 7.2. X -ray diffraction line broadening studies in inorganic powders by Morosin and co-workers show evidence for large plastic deformation with residual strain characteristic of cold-worked metals [86M02].

Toward a Taxonomy of the Denatured State Small Angle Scattering Studies of Unfolded Proteins by Millett et al. assesses denatured states induced by heat, cold, and solvent for evidence of residual structure, while Insights into the Structure and Dynamics of Unfolded Proteins from NMR by Dyson and Wright describes their extensive investigations of residual structure in the unfolded state. 

The thermal stability of metmyoglobin and apomyoglobin has been extensively studied under different solvent conditions (Privalov et al., 1986). In particular, it was shown that at low pH values both the heat and cold denaturation peaks are clearly visible in the calorimetric scans. Figure 10 shows the excess heat capacity function for apomyoglobin predicted by the hierarchical partition function and the thermodynamic parameters described above. In order to simulate the experimental curve obtained at pH 3.83 (Privalov et al., 1986), the protonation of five specific histidine residues on unfolding was... 

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