Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9770329 | Journal of Molecular Structure | 2005 | 4 Pages |
Abstract
In order to develop the design rules for producing specific conformations of peptides with α, β-dehydro-residues a peptide Cbz-ÎVal-ÎPhe-Ala-OCH3 was synthesized in solution phase. The crystal structure has been determined by X-ray diffraction method. The structure was refined to an R-value of 0.050. The peptide adopts a type I β-turn conformation with backbone torsion angles of two corner residues, Ï1=â53.9(6)°, Ï1=â33.0(6)°, Ï2=â73.7(5)° and Ï2=â12.2(6)°. The conformation is stabilized by an intramolecular 4â1 hydrogen bond involving NH of Ala residue as a donor and carbonyl oxygen atom of Cbz group as an acceptor. The torsion angles, Ï11,1=172.8(6) and Ï11,2=â6.9(9) of ÎVal residue indicate that its side chain is planar while the torsion angles, Ï21=â9.0(9), Ï22,1=â43.4(10) and Ï22,2=130.1(9) show that the side chain of ÎPhe deviates considerably from the planarity. This is the first sequence in which ÎVal and ÎPhe are introduced at adjacent positions and the structure reveals clearly that the side chain of ÎPhe is a relatively less rigid than that of ÎVal. The molecules are packed in columns parallel to c-axis.
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Authors
Vijay Kumar Goel, Sharmistha Dey, Tej P. Singh,