The x-ray diffraction analysis of the N-benzyloxycarbonyl homo-tripeptide from α-amino-isobutyric acid has shown the occurrence of an incipient 310-helix characterized by one type-III (or type-III′) β-bend followed by one oxy-analog of the same type of β-bend. This represents the first unequivocal observation of the latter conformation, where the O—H group of the COOH moiety present at the C-terminus of the peptide main chain plays the role of the hydrogen-bonding donor.

A novel peptide conformation: First unequivocal observation of the oxy-analog of a beta-bend / C., Toniolo; G., Valle; Gm, Bonora; M., Crisma; F., Formaggio; A., Bavoso; E., Benedetti; B., Di Blasio; Pavone, Vincenzo; C., Pedone. - In: BIOPOLYMERS. - ISSN 0006-3525. - STAMPA. - 25:(1986), pp. 2237-2253. [10.1002/bip.360251203]

A novel peptide conformation: First unequivocal observation of the oxy-analog of a beta-bend

PAVONE, VINCENZO;
1986

Abstract

The x-ray diffraction analysis of the N-benzyloxycarbonyl homo-tripeptide from α-amino-isobutyric acid has shown the occurrence of an incipient 310-helix characterized by one type-III (or type-III′) β-bend followed by one oxy-analog of the same type of β-bend. This represents the first unequivocal observation of the latter conformation, where the O—H group of the COOH moiety present at the C-terminus of the peptide main chain plays the role of the hydrogen-bonding donor.
1986
A novel peptide conformation: First unequivocal observation of the oxy-analog of a beta-bend / C., Toniolo; G., Valle; Gm, Bonora; M., Crisma; F., Formaggio; A., Bavoso; E., Benedetti; B., Di Blasio; Pavone, Vincenzo; C., Pedone. - In: BIOPOLYMERS. - ISSN 0006-3525. - STAMPA. - 25:(1986), pp. 2237-2253. [10.1002/bip.360251203]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/475189
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