By C B Anfinsen
ADVANCES IN PROTEIN CHEMISTRY VOL 4.
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Extra resources for Advances in Protein Chemistry, 4
The values of G/c2fall close to the curve throughout the temperature range shown. However, the fact that the melting point does depend on concentration means that the curves for different concentrations must diverge just below the melting point, where the rigidity becomes quite small. This region remains t o be investigated in detail. Dependence of Rigidity on Molecular Weight. The rigidities at 5, 10, and 15°C. /liter of gelatin are plotted against the number-average molecular weight in Fig. 12 (Ferry, 1948); these are the samples studied by Scatchard, Oncley, Williams, and Brown (1944).
Hatschek (1921) found that when a 10% gel was deformed and maintained in a state of constant strain for five days, the stress relaxed, SO that the sample kept its deformed shape even after release of the load (see Section a, page 31). However, the strain double refraction remained. This result can also be explained on the basis of orientation of structural elements, as will be discussed in more detail in Section 4, page 44. The double refraction of swollen gelatin-gels was also studied b y Quincke (1904).
5", there is a large decrease in the numerical value of rotation, which, in the case of bromides and iodides, as well as lithium chloride, falls to the value characteristic of the hightemperature form of gelatin when the salt concentration is sufficiently high. The effectiveness of ions in changing the specific rotation followed PROTEIN GELS 39 the Hofmeister series, as in the melting point studies described above. 5". 2 M for lithium chloride. Dependence of Optical Rotation on Other Added Substances.
Advances in Protein Chemistry, 4 by C B Anfinsen