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The effect of the L-azetidine-2-carboxylic acid residue on protein conformation. II. Homopolymers and copolymers

✍ Scribed by Adriana Zagari; George Némethy; Harold A. Heraga

Publisher
Wiley (John Wiley & Sons)
Year
1990
Tongue
English
Weight
493 KB
Volume
30
Category
Article
ISSN
0006-3525

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✦ Synopsis

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(Aze~3~‐Pro~3~), 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.

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