Jain, RM and Rajashankar, KR and Ramakumar, Suryanarayanarao and Chauhan, VS (1997) First Observation of Left-Handed Helical Conformation in a Dehydro Peptide Containing Two l-Val Residues. Crystal and Solution Structure of Boc-l-Val-ΔPhe-ΔPhe-ΔPhe-l-Val-OMe. In: Journal Of The American Chemical Society, 119 (14). pp. 3205-3211.
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The solution and solid structure of Boc-L-Val-Delta Phe-Delta Phe-Delta Phe-L-Val-OMe, containing three consecutive Delta Phe residues, have been determined by X-ray diffraction, nuclear magnetic resonance, and circular dichroism methods. The crystals grown from aqueous methanol are orthorhombic, space group P2(1)2(1)2(1), a = 11.624(2), b = 17.248(2), c = 21.532 Angstrom, V = 4216 (1) Angstrom(3), Z = 4. In the solid state, the peptide exhibits a left-handed 3(10)-helical conformation, in spite of the presence of two L-Val residues. NMR and CD studies in different solvents also support the crystal structure data, suggesting that the solid state structure is maintained in solution as well. This is the first report of a dehydropeptide containing three consecutive Delta Phe residues and exhibiting left-handed 3(10)-helical conformation, which demonstrates the remarkable conformational consequences produced by consecutive occurrence of Delta Phe residues in a peptide.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to American Chemical Society|
|Keywords:||X-ray diffraction;H-1 NMR;dehydropeptide;circular dichroism|
|Department/Centre:||Division of Physical & Mathematical Sciences > Physics|
|Date Deposited:||21 Jul 2009 11:27|
|Last Modified:||19 Sep 2010 05:26|
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