ISSN:
1075-2617
Keywords:
(αMe) amino acids
;
CD spectroscopy
;
310-helix
;
peptide 3D-structure
;
X-ray structure
;
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
Notes:
The terminally blocked tetrapeptide pBrBz-[D-(αMe)Leu]2-D-(αMe)Val-D-(αMe)Leu-OtBu is folded in the crystal state in a left-handed 310-helical structure stabilized by two consecutive 1 ← 4 C=O⃛H—N intramolecular H-bonds, as determined by X-ray diffraction analysis. A CD study strongly supports the view that this conformation is also that largely prevailing in MeOH solution. A comparison with the published conformation of pBrBz-[D-(αMe)Leu]4-OtBu indicates that incorporation of a single internal β-branched (αMe)Val guest residue into the host homo-tetrapeptide from the γ-branched (αMe)Leu residue is responsible for a dramatic structural perturbation, i.e. an inversion of the 310 screw sense from right to left-handed.
Additional Material:
2 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/psc.310010607
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