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Conformational Analysis of β-Turn Structure in Tetrapeptides Containing Proline or Proline Analogs

✍ Scribed by Takashi Hayashi*; Tomohito Asai; Hisanobu Ogoshi*

Publisher: Elsevier Science
Year: 1997
Tongue: French
Weight: 526 KB
Volume: 38
Category: Article
ISSN: 0040-4039
DOI: 10.1016/s0040-4039(97)00529-7

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✦ Synopsis

In order to evaluate the influenceof cyclic secondaryamino acids on the stability of ~-turn structure,we have preparedAc-Gly-L-Xxx-L-Leu-Gly -N(CH3)2(Xxx= Aze, 4-memberedring: 1, Xxx = Pro, 5-memberedring: 2, Xxx = Pip, 6-memberedring: 3). The NOE cross peaks that support $turn structure were observedin 1-3. The NOE cross peak betweenboth terminalsof the syntheticpeptides, however,was observedonly in the NOESYspectraof 2. This result indicatesthat 5-memberedring side chain in prolineplays a veryimportantrole in the formationof ~-hairpinstructure. @ 1997Elsevier ScienceLtd.

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