Abstract
The proton magnetic resonance features of poly-(N-γ-carbobenzoxy-L-α-γ-diaminobutyric acid) are consistent with a special secondary structure of this polymer when compared with the structure of its higher homologs and of other uncharged polypeptides in the same solvent systems. The pure conformational shift of the peptide α-CH proton in going from helix to random coil is for the first time isolated from the solvent shift.
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