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  • 1
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Biopolymers 11 (1972), S. 1593-1605 
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Far-infrared spectra were measured for the sequential copolymers of amino acids with alkyl group side chains. The analysis of the spectra showed that (L-Ala-L-Ala-Gly)n, (L-Ala-Gly)n, (L-Ala-Gly-Gly)n, (L-Val-L-Ala-L-Ala)n, and (L-Val-L-Ala)n, have the antiparallel pleated sheet structures and that the backbone conformations of (L-Val-L-Val-L-Ala)n and (L-Val-L-Val-Gly)n are the same as that of poly-L-valine. The far-infrared bands characteristic of the antiparallel pleated sheet structure were assigned on the basis of the result of the normal coordinate analysis of poly-L-alanine with this structure. The intersheet and interchain spacings of the sequential copolymers with the antiparallel pleated sheet structure were determined from the x-ray powder-diffraction patterns of these samples.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Biopolymers 12 (1973), S. 921-929 
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The sequential copolymers of glycine and L-alanine, L-valine and L-alanine, L-leucine and L-alanine, and L-phenylalanine and L-alanine and those containing the L-proline residues were synthesized. The infrared spectra in the region from 700 to 200 cm-1 were measured for these polypeptides with the α-helical conformation or the polyglycine II structure and compared with the spectra of the β-form structures. The results showed that several infrared bands observed in the region from 600 to 200 cm-1 clearly reflect not only the backbone conformations but also the local conformations of component amino acid residues of polypeptides with the α-helical, β-form and polyglycine II structures.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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