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Normal mode spectrum of the parallel‐chain β‐sheet
Author(s) -
Bandekar Jagdeesh,
Krimm S.
Publication year - 1988
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360270603
Subject(s) - antiparallel (mathematics) , chemistry , beta sheet , amide , raman spectroscopy , chain (unit) , dipole , coupling (piping) , crystallography , stereochemistry , materials science , physics , organic chemistry , protein structure , composite material , optics , biochemistry , quantum mechanics , astronomy , magnetic field
Normal mode calculations have been carried out for parallel‐chain β‐sheet structures. These include the parallel‐chain pleated sheet of poly( L ‐alanine) and the parallel‐chain rippled sheet of polyglycine. Dipole derivative coupling has been included for amide I and II modes, and the effects of parallel‐sheet and antiparallel‐sheet arrangements of varying separation have been examined for the poly( L ‐alanine) case. Some amide and nonamide modes are distinctly different from their antiparallel‐chain counterparts, thus providing a basis for distinguishing between such structures from their ir and Raman spectra. As in our previous studies, these results emphasize the need for both kinds of spectral data in order to draw definitive conclusions about conformation.