Abstract
Collagen is the most abundant protein in animals. In connective tissue, is present as chains wound in tight triple helices, which are organized into fibrils great tensile strength and thermal stability [1,2]. 'We have identified a new component of this stability. Collagen consists of XaaYaaGly repeats where Xaa is often L-proline (Pro) and Yaa is often 4(R)-hydroxY-L-proline (Hyp). The Hyp residues in a (ProHypGlY)1l triple helix confer substantial additional thermal stability relative to a (ProProGIY)n triple helix. It has been proposed that the extra stability ensues il'om a network of water bridges in which the 4(R)-hydroxyl group participates [1,3]. \Vater bridges that link a Hyp sidechain of one strand to a main-chain carbonyl of another strand have been seen in a crystalline collagen mimic. We believe that \vater bridges are unllkely to contribute significantly to triple-helical stability [4,5].
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