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Conformational studies of hexapeptides containing two dehydroamino acid residues in positions 3 and 5 in peptide chain

✍ Scribed by Rafal Latajka; Michal Jewginski; Maciej Makowski; Artur Krezel

Publisher
Elsevier Science
Year
2008
Tongue
English
Weight
377 KB
Volume
892
Category
Article
ISSN
0022-2860

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## Abstract The conformational preferences of the 3,3‐disubstituted β‐amino acid residue, 1‐aminocyclohexaneacetic acid (β^3,3^Ac~6~c) have been investigated by determining the crystal structures of the parent amino acid, the hydrochloride derivative, 10 protected derivatives and di and tripeptides

Erratum: “Conformations of β-amino acid
Erratum: “Conformations of β-amino acid residues in peptides: X-ray diffraction studies of peptides containing the achiral residue 1-aminocyclohexaneacetic acid, β3,3Ac6c”
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The author has brought to our attention the following revision for Table II of the article listed above, published in Biopolymers 2008, 90(2):138-150. See the revised table shown on the following page.

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The dehydro-residue containing peptides N-Ac-dehydro-Phe-L-Leu-OCH3 ( I ) and N-Acdehydro-Phe-NorVal-OCH, (11) were synthesized by the usual workup procedures. The peptides crystallize from their solutions in methanol in space group P6,: ( I ) a = b = 12.528(2) A, c = 21.653(5) A; (11) a = b = 12.53