Peptide secondary structure: An octapeptide with three TOAC (2,2,6,6-tetramethyl-1-oxyl-4-amino-4-carboxylic acid) residues forms a 310-helix in the crystal state. The three nitroxide radicals are placed in a linear configuration (see picture). As determined by electron paramagnetic resonance (EPR) spectroscopy, this secondary structure is preserved in solvents of low polarity, while in polar solvents the regularity of the 310-helix is disrupted.
Linear Configuration of the Spins of a Stable Trinitroxide Radical Based on a Ternary Helical Peptide.
CORVAJA, CARLO;FORMAGGIO, FERNANDO;TONIOLO, CLAUDIO
2005
Abstract
Peptide secondary structure: An octapeptide with three TOAC (2,2,6,6-tetramethyl-1-oxyl-4-amino-4-carboxylic acid) residues forms a 310-helix in the crystal state. The three nitroxide radicals are placed in a linear configuration (see picture). As determined by electron paramagnetic resonance (EPR) spectroscopy, this secondary structure is preserved in solvents of low polarity, while in polar solvents the regularity of the 310-helix is disrupted.
File in questo prodotto:
Non ci sono file associati a questo prodotto.
Pubblicazioni consigliate
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
