The effect of the L-azetidine-2-carboxylic acid residue on protein conformation. II. Homopolymers and copolymers.
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.
Zagari
A
A
Dipartimento di Chimica, Università di Napoli, Italy.
Némethy
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G
Scheraga
H A
HA
D001383:Azetidinecarboxylic Acid / Q000494:pharmacology*; D046911:Macromolecular Substances; D011487:Protein Conformation
D046911:Macromolecular Substances; D001383:Azetidinecarboxylic Acid