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• W1587796213 abstract "Abstract A violet-pink complex may be crystallized at high pH from a solution containing Cu2+ ions and the pentapeptide, tetraglycylglycine. A three-dimensional x-ray crystal structure analysis has shown that the complex is disodium tetraglycylglycinatocuprate(II) 4.5-hydrate, Na2[Cu(NH2— (CH2CON)3—CH2CONHCH2COO)]·4.5H2O. The crystals are triclinic, a = 7.306 A, b = 10.902 A, c = 12.012 A, α = 91.73°, β = 103.64°, γ = 96.14°, Z = 2, Dm = 1.76 ± 0.02, Dx = 1.76 g·cm-3, space group P1. The intensities of 3003 x-ray reflections were recorded by counter methods. The structure was refined to a conventional residual R = 0.080. The copper atom has coordination number four and a square planar configuration. It is bound to the peptide at the terminal N(amino) and the first three N(peptide) atoms. The amide protons are dissociated from the three metal-binding peptide groups. The fourth peptide group is not deprotonated. Neither it nor the terminal carboxyl group plays any part in the metal binding. The carboxyl group is so oriented that it accepts a weak hydrogen bond from the terminal amino group of the same peptide. In the crystal, complexes related by centers of symmetry form dimers linked by two hydrogen bonds, from the free N(peptide) in each complex to an O(peptide) in the other. In each complex the O(peptide) which is involved in this hydrogen bond is also the atom which makes the closest nonbonding contact (3.17 A) with the copper in the other half of the dimer. The Na+ ions are surrounded by octahedra of oxygen atoms belonging partly to H2O molecules and partly to peptide and carboxyl groups. The octahedra share edges to form blocks of four. The blocks are stacked on top of one another to form columns, and these columns separate regions of the crystal in which the complex anions are stacked." @default.
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• W1587796213 date "1970-10-01" @default.
• W1587796213 modified "2023-09-28" @default.
• W1587796213 title "Crystallographic Studies of Metal-Peptide Complexes" @default.
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• W1587796213 doi "https://doi.org/10.1016/s0021-9258(18)62739-5" @default.
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