Structural characterization of the. beta.-bend ribbon spiral: crystallographic analysis of two long (L-Pro-Aib) n sequential peptides
Journal of the American Chemical Society, 1992•ACS Publications
The molecular and crystal structures of two terminally blocked (L-Pro-Aib)„(«= 3, 4)
sequential peptides were determined by X-ray diffraction. In both crystals two molecules in
the asymmetricunit are found. Either molecule in the asymmetric unit of each structure shows
a right-handed/3-bend ribbon spiral, stabilized by the maximum possible number of
intramolecular NH—0= Ch-bonds. Thus, for the first time it was possible to characterize at
atomic resolution this polypeptide conformation.
sequential peptides were determined by X-ray diffraction. In both crystals two molecules in
the asymmetricunit are found. Either molecule in the asymmetric unit of each structure shows
a right-handed/3-bend ribbon spiral, stabilized by the maximum possible number of
intramolecular NH—0= Ch-bonds. Thus, for the first time it was possible to characterize at
atomic resolution this polypeptide conformation.
Abstract
The molecular and crystal structures of two terminally blocked (L-Pro-Aib)„(«= 3, 4) sequential peptides were determined by X-ray diffraction. In both crystals two molecules in the asymmetricunit are found. Either molecule in the asymmetric unit of each structure shows a right-handed/3-bend ribbon spiral, stabilized by the maximum possible number of intramolecular NH—0= Ch-bonds. Thus, for the first time it was possible to characterize at atomic resolution this polypeptide conformation.
ACS Publications