Download Advances in Protein Chemistry, 4 by C B Anfinsen PDF

By C B Anfinsen

ADVANCES IN PROTEIN CHEMISTRY VOL 4.

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6 g. water per g. , the difference between the total heat which would be absorbed between these two temperatures and that attributable to the heat capacities in the absence of a thermal transition. I 28 JOHN D. FERRY A smaller number of measurements a t other temperatures permitted estimates of curves of the integral heat of wetting, shown as dashed lines in Fig. 9. 5% by weight. In other words, if a gel of this concentration were warmed, the absorption of heat accompanied by disruption of structure would begin a t about 16".

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).

Unlike most aqueous gels, these are thixotropic, and their structure may be somewhat different. f . Optical Rotation. The change in optical rotation with time during gelation has already been mentioned (page 22). The equilibrium value FIG. 14. Light scattering by 1% gelatin solutions, plotted against pH. I, 17"; 11, 23'; 111, 30'; IV, 40" and 50". From Kraemer and Dexter (1927). of optical rotation (taken after the initial rapid change is completed but before the subsequent slow change has progressed appreciably) was found by Smith (1919) to depend upon both concentration and temperature.

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