By C B Anfinsen
ADVANCES IN PROTEIN CHEMISTRY VOL 4.
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Additional info for Advances in Protein Chemistry, 4
Among the molecules of various lengths which are present in any real gelatin sample as degradation products, the longer species might also be expected to participate in network formation, while the shorter species would be unable to do so. , indicating rather close juxtaposition of polypeptide chains. Hence the rigidity of a gelatin gel may be attributed with some confidence to the presence of a network. PROTEIN GELS 41 There is also strong, although indirect, evidence that the gelatin network is of the type described in Section 111, 2, page 10-that the individual molecular chains are bound together by secondary attractive forces localized at widely separated points.
8-A. and 8-A. spacings are meridional and the 12-A. spacing equatorial (Herrmann, Gerngross, and Abitz, 1930; Derksen, 1935). 8 A. 5 A. 5 A. over a concentration range from 70 % to 30 %. 0 A. 86 A. , dry (Astbury, 1940). It is apparent that gelation in these highly concentrated gels (concentration > 30%) is accompanied by the formation of ordered fibrous arrangements resembling those originally present in collagen. The side-chain spacings are similar, indicating in both cases a slight separation of the chains in the presence of water; and the identity periods along the fiber axis are the same.
Qualitatively a range of melting can also be explained in terms of the entropy changes as increased crystallization causes more and more constraint of the chains between crystallites, following the treatment of Alfrey and Mark (1942), or Frith and Tuckett (1944). An alternative postulate to that of Gerngross is that the initial formation of a gel is due to associations between chains in pairs rather than in bundles; ‘that the cross-links in gels when first set, and particularly in dilute gels, are single rather than multiple.
Advances in Protein Chemistry, 4 by C B Anfinsen