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Direct determination of helix structures involved in the screw-sense reversal of poly(β-phenylpropyl l-aspartate) by synchrotron X-ray diffraction.

Authors :
Orito Y
Masunaga H
Furuya H
Abe A
Source :
Journal of peptide science : an official publication of the European Peptide Society [J Pept Sci] 2021 Jun; Vol. 27 (6), pp. e3311. Date of Electronic Publication: 2021 Feb 18.
Publication Year :
2021

Abstract

The helix-sense reversal of poly(β-phenylpropyl l-aspartate) (3PLA) in the solid state was studied by synchrotron wide-angle X-ray diffraction and small-angle X-ray scattering. The direct determination of the characteristic helical pitch before and after the transition revealed that the transition takes place reversibly between the two α-helices having opposite screw-sense during the heating and cooling cycle. While the hexagonal packing remains unaltered, the helix-sense inversion causes discontinuous changes in the molecular arrangement and, by extension, the crystalline dimension. In this study, another transition was detected at a higher temperature from the left-handed α-helix to the π-helix, the molecular chirality being unaffected.<br /> (© 2021 European Peptide Society and John Wiley & Sons, Ltd.)

Details

Language :
English
ISSN :
1099-1387
Volume :
27
Issue :
6
Database :
MEDLINE
Journal :
Journal of peptide science : an official publication of the European Peptide Society
Publication Type :
Academic Journal
Accession number :
33605058
Full Text :
https://doi.org/10.1002/psc.3311