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- W2111444386 abstract "Observations of extended peptide chains, whose direction is perpendicular to the fiber axis (cross-beta-structures) have hitherto been confined to fibrous proteins and to some synthetic polydisperse polypeptides of rather low molecular weight. This structure has now been found in some monodisperse linear homo-oligopeptides with aliphatic hydrocarbon side chains. X-ray diffraction photographs of t-Boc-(D-Ala)7-OMe and HCl.H(D-Ala)7-OMe show characteristic reflections for this form. In addition, the good orientation of suitably prepared specimens has enabled a fairly complete determination of the unit cell of the heptapeptides to be made. t-Boc-(D-Ala)7-OMe and HCl.H(D-Ala)7-OMe molecules are packed in a monoclinic lattice with a = 4.80, b = 34.5, c = 5.82 A, beta = 65.6 degrees and a = 4.80, b = 29.5, c = 5.82 A, beta = 65.6 degrees, respectively. It has not been possible to establish whether the arrangement of the chains within the sheets is parallel or antiparallel." @default.
- W2111444386 created "2016-06-24" @default.
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- W2111444386 date "2009-01-12" @default.
- W2111444386 modified "2023-09-27" @default.
- W2111444386 title "X-RAY STUDY ON HOMO-OLIGOPEPTIDES t-BOC-(d-Ala)7-OMe AND HCI·H(d-Ala)7-OMe" @default.
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- W2111444386 doi "https://doi.org/10.1111/j.1399-3011.1979.tb01895.x" @default.
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