Search results for "Methylamide"
showing 8 items of 28 documents
CCDC 202882: Experimental Crystal Structure Determination
2004
Related Article: D.Siodlak, M.A.Broda, B.Rzeszotarska, E.Kolodziejczyk, A.E.Koziol|2004|Z.Kristallogr.|219|231|doi:10.1524/zkri.219.4.231.30447
CCDC 862035: Experimental Crystal Structure Determination
2017
Related Article: Dawid Siodłak, Agnieszka Macedowska-Capiga, Małgorzata A. Broda, Anna E. Kozioł, Tadeusz Lis|2012|Biopolymers|98|466|doi:10.1002/bip.22082
CCDC 192132: Experimental Crystal Structure Determination
2003
Related Article: B.Rzeszotarska, D.Siodlak, M.A.Broda, I.Dybala, A.E.Koziol|2002|J.Pept.Res.|59|79|doi:10.1034/j.1399-3011.2002.10951.x
The conformation cis of N-acetyl-N-methyl-α,β-dehydroalanine N′-methylamide and saturated analogues
2007
A series of three homologous amino acids derivatives: N-acetyl-N-methyl-α,β–dehydroalanine N′-methylamide (1), N-acetyl-N-methyl-L-alanine N′-methylamide (2), and N-acetyl-N-methyl-DL-alanine N′-methylamide have been synthesised. The racemic species undergoes spontaneous separation into L and D-enantiomers. From these two chiral forms, the structure of L-enantiomer (3) was analysed. The molecules of 1 – 3 adopt the cis arrangement of the N-terminal amide bond. The molecular conformations are similar for 1 (φ, ψ = 94.6(1)°, −1.7(1)°) and 3 (φ, ψ = 111.5(1)°, −23.8(1)°), and also 2 (φ, ψ = −114.8(2)°, 29.5(2)°), if inversion through the chiral C2 carbon is considered. They are stabilised by i…
Conformational investigation of α,β-dehydropeptides. IX. N-Acetyl-(E)-α,β-dehydrobutyrine N′-methylamide: stereoelectronic properties from infrared a…
2009
The Fourier transform infrared spectra of Ac-(E)-deltaAbu-NHMe were analyzed to determine the predominant solution conformation(s) of this (E)-alpha,beta-dehydropeptide-related compound and the electron density perturbation in its amide groups. The measurements were performed in dichloromethane and acetonitrile in the region of mode vs (N-H), amide I, amide II and vs (C(alpha)=Cbeta). The equilibrium geometrical parameters, calculated by a method based on the density functional theory with the B3LYP functional and the 6-31G* basis set, were used to support spectroscopic interpretation and gain some deeper insight into the molecule. The experimental and theoretical data were compared with th…
Conformational properties of N-acetyl-N-methyl-alpha,beta-dehydroalanine N'-methylamide.
2006
The conformational properties of Ac-Delta(Me)Ala-NHMe (N-acetyl-N-methyl-alpha,beta-dehydroalanine N'-methylamide), as the simplest model of N-methyl-alpha,beta-dehydroamino acids, was examined with theoretical methods and in comparison with Ac-DeltaAla-NHMe and Ac-DeltaAla-NMe(2). The N-terminal amide of the Delta(Me)Ala residue easily adopts the configuration cis and the torsion angles phi, psi are highly flexible. The Delta(Me)Ala residue is a conformational flexibilizer as compared to the parent DeltaAla, which is a conformational stiffener. This seems to be the reason why Delta(Me)Ala is found in small natural cyclic peptides, where it ensures the conformational flexibility necessary f…
N-Methyldehydroamino acids promote a configuration cis of N-methylamide bond
2008
Abstract Dehydroamino acids with a methylated N-terminal tertiary amide bond occur in natural small cyclic peptide toxins. To investigate their conformational preferences a systematic theoretical analysis was performed on N ′-methylamides of N -acetyl- N -methyldehydroamino acids (Ac-Δ(Me)Xaa-NHMe, where Xaa = ( Z )-Abu, ( E )-Abu, Val, ( Z )-Phe, and ( E )-Phe) considering the configuration trans and cis of the tertiary amide bond. The ϕ , ψ potential energy surfaces were calculated at the B3LYP/6-31+G ∗∗ //HF/3-21G level with inclusion of the solvent (water) effect (SCRF method). The conformers localised were fully optimised at the B3LYP/6-31+G ∗∗ in vacuo. The accessible areas of the pot…
Conformational investigation of α, β-dehydropeptides
2009
The crystal structure of Ac-Pro-delta Val-NHCH3 was examined to determine the influence of the alpha,beta-dehydrovaline residue on the nature of peptide conformation. The peptide crystallizes from methanol-diethyl ether solution at 4 degrees in needle-shaped form in orthorhombic space group P2(1)2(1)2(1) with a = 11.384(2) A, b = 13.277(2) A, c = 9.942(1) A, V = 1502.7(4) A3, Z = 4, Dm = 1.17 g.cm-3 and Dc = 1.18 g.cm-3. The structure was solved by direct methods using SHELXS-86 and refined to an R value of 0.057 for 1922 observed reflections. The peptide is found to adopt a beta-bend between the type I and the type III conformation with phi 1 = -68.3(4) degrees, psi 1 = -20.1(4) degrees, p…