The solid state conformational analysis of [Tyr4] cyclolinopeptide A has been carried out by x‐ray diffraction studies. The crystal structure of the monoclinic form, grown from a dioxane‐water mixture [a = 9.849 (5) Å, b = 20.752 (4) Å, c = 16.728 (5) Å, β = 98.83 (3)°, space group P21, Z = 2], shows the presence of five intramolecular N‐H OC hydrogen bonds, with formation of one C17 ring structure, one α‐turn (C13), one inverse γ‐turn (C7), and two β‐turns (C10, one of type III and one of type 1). The Pro1‐Pro2 peptide unit is cis (ω = 5°) all others are trans. The structure is almost superimposable with that of cyclolinopeptide A. The rms deviation for the atoms of the backbones is on the average 0.33 Å. © 1995 John Wiley & Sons, Inc. Copyright © 1995 John Wiley & Sons, Inc.
Bioactive peptides: Conformational studies of [TYR4] cyclolinopeptide A
ISERNIA, Carla;
1995
Abstract
The solid state conformational analysis of [Tyr4] cyclolinopeptide A has been carried out by x‐ray diffraction studies. The crystal structure of the monoclinic form, grown from a dioxane‐water mixture [a = 9.849 (5) Å, b = 20.752 (4) Å, c = 16.728 (5) Å, β = 98.83 (3)°, space group P21, Z = 2], shows the presence of five intramolecular N‐H OC hydrogen bonds, with formation of one C17 ring structure, one α‐turn (C13), one inverse γ‐turn (C7), and two β‐turns (C10, one of type III and one of type 1). The Pro1‐Pro2 peptide unit is cis (ω = 5°) all others are trans. The structure is almost superimposable with that of cyclolinopeptide A. The rms deviation for the atoms of the backbones is on the average 0.33 Å. © 1995 John Wiley & Sons, Inc. Copyright © 1995 John Wiley & Sons, Inc.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
