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Variations I–XVIII of a trimerlike cross‐linked collagen model peptide were synthesized and used to investigate the cooperation of different neighboring Gly‐X‐Y tripeptides. The carboxy‐terminal decapentapeptide of the tripe‐helical part of collagen type I was chosen as the starting point of sequentially modified elongations. The transition temperatures determined by CD measurements show that the incorporation of the imino acid free tripeptides Gly‐Ala‐Ala and Gly‐Ile‐Ala results in a weakening of the triple‐helical structure. It is demonstrated that the desired thermal stability of the collagen triple helix requires the “clustered” arrangement of helix‐promoting tripeptides, especially of Gly‐Pro‐Hyp.
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Germann et al. (1988) studied this question.
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