The infrared absorption and 'H nuclear magnetic resonance analyses of chloroform solutions of the terminally blocked homooctapeptide from the C,+-dimethylated a-aminoisobutyric acid residue are consistent with the presence of a 310-helical structure of high thermal stability. The crystal structure of the octapeptide, obtained by X-ray diffraction, indicates the formation of a 310-helix, stabilized by six consecutive intramolecular N-H-O=C H bonds of the Clo-I11 (or 111') type. This represents the first observation at atomic resolution of a regular 310-helix larger than two complete tums. Packing of the octapeptide molecules gives rise to a channel in which the solvent (methanol and water) molecules are accommodated.
LINEAR OLIGOPEPTIDES .143. A LONG, REGULAR POLYPEPTIDE 3(10)-HELIX / C., Toniolo; G., Bonora; A., Bavoso; E., Benedetti; B., DI BLASIO; Pavone, Vincenzo; C., Pedone. - In: MACROMOLECULES. - ISSN 0024-9297. - STAMPA. - 19:(1986), pp. 472-479.
LINEAR OLIGOPEPTIDES .143. A LONG, REGULAR POLYPEPTIDE 3(10)-HELIX
PAVONE, VINCENZO;
1986
Abstract
The infrared absorption and 'H nuclear magnetic resonance analyses of chloroform solutions of the terminally blocked homooctapeptide from the C,+-dimethylated a-aminoisobutyric acid residue are consistent with the presence of a 310-helical structure of high thermal stability. The crystal structure of the octapeptide, obtained by X-ray diffraction, indicates the formation of a 310-helix, stabilized by six consecutive intramolecular N-H-O=C H bonds of the Clo-I11 (or 111') type. This represents the first observation at atomic resolution of a regular 310-helix larger than two complete tums. Packing of the octapeptide molecules gives rise to a channel in which the solvent (methanol and water) molecules are accommodated.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
