Publication | Closed Access
Linear oligopeptides. Part 227. X-Ray crystal and molecular structures of two α-helix-forming (Aib-<scp>L</scp>-Ala)sequential oligopeptides, pBrBz-(Aib-<scp>L</scp>-Ala)<sub>5</sub>-OMe and pBrBz-(Aib-<scp>L</scp>-Ala)<sub>6</sub>-OMe
42
Citations
23
References
1990
Year
X-ray CrystallographyCrystal StructureEngineeringBiomolecular Structure PredictionMolecular BiologyPeptide ScienceAnalytical UltracentrifugationChemical BiologySequential OligopeptidesProtein X-ray CrystallographyStructure ElucidationMacromolecular AssembliesProtein ChemistryBiochemistry6-Ome DihydrateLinear OligopeptidesMolecular Modeling5-Ome TetrahydrateCrystallographyStructural BiologyBiomolecular EngineeringX-ray CrystalNatural SciencesX-ray Diffraction
A crystal-state structutal analysis of pBrBz-(Aib-LAla)5-OMe tetrahydrate and pBrBz-(Aib-L-Ala)6-OMe dihydrate has been performed by X-ray diffraction. The decapeptide and dodecapeptide molecules are both basically α-helical with five and seven 1 â†� 5 intramolecular H-bonds, respectively. A similarity between the two structures is also seen near the C-terminus, where regularity of the α-helix is disrupted in favour of formation of intramolecular H-bonds of the 1 â†� 4 and 1 â†� 6 types. A brief comparison with parameters and interactions characteristic of the helices present in globular proteins has been made.
| Year | Citations | |
|---|---|---|
Page 1
Page 1