Abstract
Peptides and polypeptides comprising the sequence X-Gly-Gly (X=Val, Ala, Leu) have been synthesized by classical methods. They represent either analogs or fragments of the prolyl devoid sequences of elastin. The conformation of the peptides has been studied in a wide range of conditions by using CD and mono- and two-dimensional proton NMR. The obtained results are discussed in terms of the structure and elasticity of elastin.
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