Conformational energy computations on a derivative and a homo-dipeptide of Cα,α-diethylglycine were performed. In both cases the N- and C-terminal groups are blocked as acetamido and methylamido moieties, respectively. It was found that the Cα,α-diethylglycine residues are conformationally restricted and that the minimum energy conformation corresponds to the fully extended C5 structure when the N Cα C′ bond angle is smaller than 108° (as experimentally observed).
Structural versatility of peptides from Cα, α‐dialkylated glycines. I. A conformational energy computation and x‐ray diffraction study of homo‐peptides from Cα, α‐diethylglycine / Benedetti, E.; Barone, V.; Bavoso, A.; Di Blasio, B.; Lelj, F.; Pavone, Vincenzo; Pedone, C.; Bonora, Gm; Toniolo, C.; Leplawy, Mt. - In: BIOPOLYMERS. - ISSN 0006-3525. - STAMPA. - 27:3(1988), pp. 357-371. [10.1002/bip.360270302]
Structural versatility of peptides from Cα, α‐dialkylated glycines. I. A conformational energy computation and x‐ray diffraction study of homo‐peptides from Cα, α‐diethylglycine
PAVONE, VINCENZO;
1988
Abstract
Conformational energy computations on a derivative and a homo-dipeptide of Cα,α-diethylglycine were performed. In both cases the N- and C-terminal groups are blocked as acetamido and methylamido moieties, respectively. It was found that the Cα,α-diethylglycine residues are conformationally restricted and that the minimum energy conformation corresponds to the fully extended C5 structure when the N Cα C′ bond angle is smaller than 108° (as experimentally observed).I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
