A synthetic, terminally-blocked homo-heptapeptide from alpha-aminoisobutyric acid has been studied by single-crystal X-ray diffraction and the structure refined to R = 0.05. The compound is folded into two complete turns of a regular 3(10)-helix, stabilized by five consecutive intramolecular N-H...O = C H-bonds of the beta bend III (III') type. This structure completes the series of the homo-oligomers of alpha-aminoisobutyric acid to the octapeptide level analyzed at atomic resolution by X-ray diffraction.
Linear Oligopeptides .231. Preferred Conformation of Homo-oligomers of Alpha-aminoisobutyric-acid - Molecular and Crystal-structure of Z-(aib)7-ome
FORMAGGIO, FERNANDO;TONIOLO, CLAUDIO
1991
Abstract
A synthetic, terminally-blocked homo-heptapeptide from alpha-aminoisobutyric acid has been studied by single-crystal X-ray diffraction and the structure refined to R = 0.05. The compound is folded into two complete turns of a regular 3(10)-helix, stabilized by five consecutive intramolecular N-H...O = C H-bonds of the beta bend III (III') type. This structure completes the series of the homo-oligomers of alpha-aminoisobutyric acid to the octapeptide level analyzed at atomic resolution by X-ray diffraction.File in questo prodotto:
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