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EN
The solid phase synthesis of a-hydroxymethylserine peptides is affected by accumulation of deleted sequences and NŽO-acyl migrations, occurring under acidic conditions of cleavage from Wang resin. The conformational behaviour of peptides, containing alanine host-residues separated by a single or consecutive a-hydroxymethylserine (HmS) guest-residues, has been studied by CD spectroscopy in polar protic solvents. The presence of sequential motif (Ala-HmS)n, n=2,4, shifts the conformational equilibria towards ordered structures. The CD spectrum of the nonapeptide Ac-Ala-(HmS-Ala)4-OH in trifluoroethanol is indicative of a right-handed helix. Peptides with consecutive HmSn residues, n=2,3, are apparently less ordered than those containing alternating sequences Ala-HmS. Random coil conformation is adopted by the nonapeptide Ac-Ala3-(HmS)3-Ala-OH containing three neighbouring HmS residues.
EN
The 3-cyclohexene-1-carboxylic acid was prepared and resolved with brucine. Absolute configuration of (R)-(+)-3-cyclohexene-1-carboxylic acid was confirmed by X-ray diffraction methods.
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