A synthetic, terminally blocked homodecapeptide from the Cα,α-dimethylated glycyl residue α-aminoisobutyric acid has been analyzed by single-crystal X-ray diffraction and the structure refined to R = 0.073. The compound crystallizes as a perfect 310 helix, stabilized by eight consecutive intramolecular NH ... OC hydrogen bonds. This is the first observation at atomic resolution of a regular polypeptide 310 helix as long as three complete turns. © 1990.
The longest, regular polypeptide 310 helix at atomic resolution / Pavone, Vincenzo; Di Blasio, Benedetto; Santini, Antonello; Benedetti, Ettore; Pedone, Carlo; Toniolo, Claudio; Crisma, Marco. - In: JOURNAL OF MOLECULAR BIOLOGY. - ISSN 0022-2836. - 214:3(1990), pp. 633-635. [10.1016/0022-2836(90)90279-U]
The longest, regular polypeptide 310 helix at atomic resolution
Vincenzo Pavone;Antonello Santini;Ettore Benedetti;Carlo Pedone;
1990
Abstract
A synthetic, terminally blocked homodecapeptide from the Cα,α-dimethylated glycyl residue α-aminoisobutyric acid has been analyzed by single-crystal X-ray diffraction and the structure refined to R = 0.073. The compound crystallizes as a perfect 310 helix, stabilized by eight consecutive intramolecular NH ... OC hydrogen bonds. This is the first observation at atomic resolution of a regular polypeptide 310 helix as long as three complete turns. © 1990.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
