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In vitro analysis demonstrates native-like folding of shark skin collagen type I α1 chains, highlighting structural and thermal recovery of the triple helix.
Renaturation of α1 chains from shark skin collagen (1) was measured by the increase in optical rotation and viscosity. The rotation change of the α1(1) chains became constant after 18 hr, while the viscosity increased further with time. Size exclusion chromatographic patterns of renaturation products of α1 (I) chain gave similar results to that of native collagen. The renaturation products remelted with rising temperature in a similar way to the melting of native collagen as judged from the rotation‐temperature curve.
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Nomura et al. (1995) studied this question.
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