Abstract

The unpolarised infra-red spectrum of partially deuterated collagen (bovine Achilles tendon) with the primary hydration sheath intact shows an unexpected variation in the intensity of the ND stretch upon rotation about the fibre direction. The phenomenon suggests that the intra-chain hydrogen bonds in the triple helical structure of collagen are of inequivalent strength. Intra-chain hydrogen bonds of similar bond strength appear to lie in the same plane.

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