Synthetic fragments and analogues of elastin. II. Conformational studies

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Abstract
Conformational studies on synthetic repetitive sequences and analogues of elastin are described. CD and nmr measurements gave evidence of flexible β‐turns as the dominant structural feature whose stability was found to decrease by increasing the number of repetitive units. The sequences comprised the structural unit Gly‐X‐Gly (X = Val, Leu, Ala), with X‐Gly or Gly‐Gly located at the corners of the bend. Based on that, it is proposed that these regions of elastin, unlike the proline‐containing sequences, contribute to the elasticity of the protein through a classical mechanism in terms of the rotational isomeric state theory.