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A novel peptide conformation: First unequivocal observation of the oxy‐analog of a β‐bend
Author(s) -
Toniolo Claudio,
Valle Giovanni,
Bonora Gian Maria,
Crisma Marco,
Formaggio Fernando,
Bavoso Alfonso,
Benedetti Ettore,
Di Blasio Benedetto,
Pavone Vincenzo,
Pedone Carlo
Publication year - 1986
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360251203
Subject(s) - chemistry , tripeptide , moiety , peptide , stereochemistry , hydrogen bond , isobutyric acid , crystallography , helix (gastropod) , derivative (finance) , diffraction , x ray crystallography , molecule , organic chemistry , biochemistry , ecology , physics , optics , economics , biology , snail , financial economics
The x‐ray diffraction analysis of the N‐benzyloxycarbonyl homo‐tripeptide from α‐amino‐isobutyric acid has shown the occurrence of an incipient 3 10 ‐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. These results have been compared with those of the same peptide in its monohydrate form and of its methyl ester derivative, the x‐ray diffraction structures of which are also described here.