The fully extended peptide conformation (2.0(5)-helix) has been investigated for the first time in the solid-state by C-13 cross-polarization magic angle spinning NMR. The compounds examined are members of a terminally protected, homo-oligopeptide series (from monomer through hexamer) based on C-alpha,C-beta-didehydroalanine
A study of a C-alpha,C-beta-didehydroalanine homo-oligopeptide series in the solid-state by C-13 cross-polarization magic angle spinning NMR
TONIOLO, CLAUDIO;FORMAGGIO, FERNANDO
2004
Abstract
The fully extended peptide conformation (2.0(5)-helix) has been investigated for the first time in the solid-state by C-13 cross-polarization magic angle spinning NMR. The compounds examined are members of a terminally protected, homo-oligopeptide series (from monomer through hexamer) based on C-alpha,C-beta-didehydroalanineFile in questo prodotto:
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