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The effect of the L ‐azetidine‐2‐carboxylic acid residue on protein conformation. II. Homopolymers and copolymers
Author(s) -
Zagari Adriana,
Némethy George,
Heraga Harold A.
Publication year - 1990
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360300910
Subject(s) - chemistry , copolymer , residue (chemistry) , cooperativity , polymer , polymer chemistry , polyproline helix , amino acid residue , proline , amino acid , organic chemistry , biochemistry , peptide , peptide sequence , gene
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.