The effect of theL‐azetidine‐2‐carboxylic acid residue on protein conformation. IV. Local substitutions in the collagen triple helix
作者:
Adriana Zagari,
Kathleen A. Palmer,
Kenneth D. Gibson,
George Némethy,
Harold A. Scheraga,
期刊:
Biopolymers
(WILEY Available online 1994)
卷期:
Volume 34,
issue 1
页码: 51-60
ISSN:0006-3525
年代: 1994
DOI:10.1002/bip.360340107
出版商: Wiley Subscription Services, Inc., A Wiley Company
数据来源: WILEY
摘要:
AbstractThe properties of collagen are affected by the replacement of Pro by imino acid analogues. The structural effect of the low‐level local substitution ofL‐azetidine‐2‐carboxylic acid (Aze) has been analyzed by computing the energy of CH3CO‐(Gly‐Pro‐Pro)4‐NHCH3triple helices in which a single residue of one strand has been replaced by Aze. When Aze is in position Y of a (Gly‐X‐Y) unit, low‐energy local deformations are introduced in the triple helix, i.e., it becomes more flexible. On the other hand, the flexibility of the triple helix is not increased with Aze in position X. The energy of the triple helix to coil transition is not changed significantly by this amount of substitution. In an earlier study, we have demonstrated that the regular substitution of Aze in every tripeptide distorts or destabilizes the triple helix to a large extent [A. Zagari, G. Némethy,&H. A. Scheraga (1990)Biopolymers, Vol. 30, pp. 967–974 ]. Thus, it appears that a high level of substitution is required to cause the observed chemical and biological effects of Aze on collagen. ©
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