Conformational studies of sequential polypeptides of L-Alanine and β-Alanine |
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Authors: | T. Komoto Y. Minoshima T. Kawai |
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Affiliation: | (1) Department of Polymer Technology, Tokyo Institute of Technology, Ookayama, Meguro-ku, Tokyo, Japan |
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Abstract: | Summary In order to investigate the effect of the -alanine residue on the conformational stability of -helical poly(L-alanine), studies have been made on the conformations of sequential copolypeptides having the following repeating sequences: (L-Ala--Ala)n, (L-Ala-L-Ala--Ala)n, (L-Ala--Ala-L-Ala-L-Ala)n and (L-Ala-L-Ala-X)n, where X is D,L--amino-isobutyric acid residue. Conformations of these polypeptides were measured both in the solution and solid states by means of optical rotatory dispersion, infrared and far-infrared spectroscopies and X-ray diffractions. All the copolypeptides studied here did not give the -helix. It may be, therefore, concluded that the -alanine residue is not incorporated in but impairs the -helix of poly(L-alanine), since the hydrogen bond periodicity in the -helical chain is disturbed by the introduction of such a -amino acid as -alanine.With 5 figures and 2 tables |
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