Reconstitution of collagen‐fold structure with stretching of gelatin film

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Abstract
The gelatin film is stretched more 100% over 75% relative humidity, while the dried gelatin extended only several percent. In this experiment the gelatin film was stretched in a solution of water and ethanol. The sample was extended to 650% of its initial length when ethanol/water was 1.5(w/w) at 30°C. The wide‐angle X‐ray diffraction photographs of drawn samples showed the three important layer lines with approximate spacing of 10 Å, 4 Å, and 3 Å, which verify the reconstitution of collagen triple helical structure. The sharp spots appeared near 10 Å on the equatirial axis, indicating the high orientation of peptide chains. These patterns become sharp and clear on increasing the extension ratio.The content of the triple helix was investigated by wide‐angle X‐ray diffraction and differential scanning calorimetry. The maximum renaturation percentage is 25% at the draw ratio of 7.5. Since the formation of a collagen triple helix requires three chains, in which each chain has only three repeatin amino acids, (Gly‐Pro‐X)n, and glycoprotein and other impurities interrupt helix formation, the more advanced renaturation will not be expected.