Advances in Protein Chemistry, 4 by C B Anfinsen

By C B Anfinsen

ADVANCES IN PROTEIN CHEMISTRY VOL 4.

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The amorphous ring, which is shown by both gel and solution, is considered to be the result of diffraction by the disordered portions of the chains. When a gel is stretched, the bundles or crystallites are partly aligned in the direction of stretch, accounting for the resolution of the sharp rings into a fiber pattern. According to this view, the network is formed by partial crystallization of certain regions of the chain; the evolution of heat and contraction in volume which FIG. 10. Schematic diagram of net- accompany gelation are analogous work formed by crystallites.

The high electrostatic repulsion is probably even more important than the low dielectric constant in keeping the denatured protein in solution. When the magnitude of the coulombic repulsion is diminished by presence of neutral salt, association may occur here and there between the polypeptide chains, leading to formation of a gel network. With a higher proportion of salt, gelation occurs before the denaturation process has proceeded far enough t o build up a very high concentration 50 JOHN D. FERRY of free chains, and, in accordance with the principles already outlined, a coarse, opaque gel is formed.

Rigidity and Other Mechanical Properties. The modulus of rigidity, G, the most characteristic gel property, and the related modulus of elasticity (very nearly equal to 3 G ) , can be calculated from measurements of the deformation of a gel in shear and in extension, respectively, under PROTEIN GELS 29 known stress. Blocks of material may be bent or stretched (Leick, 1904); for a weaker system, which deforms under its own weight, it is convenient to subject the material to torsion between two concentric cylinders, the outer of which serves as a container (Hatschek and Jane, 1926).

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Advances in Protein Chemistry, 4 by C B Anfinsen
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