Piazzesi, AM and Bardi, R and Crisma, M and Banora, GM and Toniolo, C and Chauhan, VS and Kaur, P and Uma, K and Balaram, P (1991) Conformational restrictions of peptides via backbone modification: Solution and crystal-state analysis of Boc-L-Pro-DZPhe-Gly-NH2. In: Gazzetta Chimica Italiana, 121 (1). pp. 1-7.
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An N-alpha-protected model tripeptide amide containing, in the central position, an alpha,beta-dehydrophenylalanine (Z-configurational isomer), Boc-L-Pro-DELTA-Z-Phe-Gly-NH2 (Boc, tert-butyloxycarbonyl), has been synthesized by solution methods and fully characterized. IR absorption and H-1 NMR studies provided evidence for the occurrence of a significant population of a conformer containing two consecutive, intramolecularly H-bonded (type II-III') beta-bends in solution. However, an X-ray diffraction analysis clearly indicates that only the type-II beta-bend structure survives in the crystal state.
|Item Type:||Journal Article|
|Additional Information:||Copy right of this article belongs to Society Chimica Italiana.|
|Department/Centre:||Division of Biological Sciences > Molecular Biophysics Unit|
|Date Deposited:||27 Apr 2010 05:30|
|Last Modified:||19 Sep 2010 06:00|
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