title: The effect of the L-azetidine-2-carboxylic acid residue on protein conformation. II. Homopolymers and copolymers.
abstract: The alteration of polymer conformational properties caused by the replacement of L-proline by L-azetidine-2-carboxylic acid (Aze) has been studied by means of conformational energy computations. In addition to poly(Aze), two sequential copolymers, poly(Pro-Aze) and poly(Aze3-Pro3), have been investigated. All polymers containing Aze are more flexible than poly(Pro). This is a consequence of an increased number of permitted conformational states for the Aze residue, as compared to Pro, when they are incorporated into a polypeptide, as well as of a lessened cooperativity of the trans-cis transition. The results of the computation can be used to interpret the observed physical properties of poly(Aze) and of its copolymers.
authors.affiliation: Dipartimento di Chimica, Università di Napoli, Italy.
authors.forename: A
authors.initials: A
authors.lastname: Zagari
authors.forename: G
authors.initials: G
authors.lastname: Némethy
authors.forename: H A
authors.initials: HA
authors.lastname: Scheraga
mesh_terms: D001383:Azetidinecarboxylic Acid / Q000494:pharmacology*; D046911:Macromolecular Substances; D011487:Protein Conformation
chemical_list: D046911:Macromolecular Substances; D001383:Azetidinecarboxylic Acid