Structure cristalline du composé PtCl<sub>6</sub>–<scp>L</scp>-lysine

L'Haridon, P.; Lang, Joseph; Pastuszak, R.; Dobrowolski, Jan Cz.

doi:10.1107/s0567740878008390

Cited by 12 publications

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References 3 publications

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“…Such large a binding energy hints strongly that lysine adsorbs on the Cu(001) surface also in its anionic form, , same as its adsorption form on Pt 26 or TiO 2 7 from solution. Actually, many amino acids adsorb on metal surfaces in their anionic form. ,− , The main chain of lysine, excluding the side chain (−(CH 2 ) 4 NH 2 ), obviously is comparable with glycine, and hence the two oxygen atoms and the nitrogen atom are expected also to stay at or near the atop site as in the case of glycine/Cu(110). − As for the conformation of the side chain −(CH 2 ) 4 NH 2 , we refer to the conformations of lysine molecule in various crystals. − Similarly, the two oxygen atoms of the formate , and acetate , on Cu(100) and (110) and the nitrogen atom of ammonia NH 3 on Cu(100) also take atop sites. , As the most favorable conformation, the side chain is all trans and thus fully extended . On the basis of above considerations, a unified model has been proposed for both the ( ) and the ( ) superstructures for further investigation (see Figure ).…”

Section: Resultsmentioning

confidence: 99%

Scanning Tunneling Microscopy Investigation of l-Lysine Adsorbed on Cu(001)

2000

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Adsorption of L-lysine (or, in absolute nomenclature, S-lysine) on Cu(001) has been studied with a UHV-STM. The binding energy is estimated to be not lower than 1.6 eV, and thus lysine is expected to be in its anionic form on the surface. The adsorbates have two phases, that is, the two-dimensional (2D) gas and solid phases. We speculate that in the 2D gas phase the molecules stand upright on the surface with their two oxygen atoms at the atop sites and can diffuse frequently, and that in the 2D solid phase the molecules lie down on the surface and connect to their neighboring molecules by hydrogen bonds so to form two slightly different superstructures, Cu(001)( -2 4 41 )-and Cu(001)( -3 4 41 )-L-lysine, for which models have been proposed for further investigation. Surprisingly, adsorption of L-lysine can make all steps restructuring into {3 1 17} facets with the same chirality. This phenomenon shows that chiral metal surfaces have potential in discrimination of molecular chirality.

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Section: Resultsmentioning

confidence: 99%

Scanning Tunneling Microscopy Investigation of l-Lysine Adsorbed on Cu(001)

2000

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“…References: (a) Koetzle, Lehmann, Verbist & Hamilton (1972): (b) Bhat & Vijayan (1976): (e) L'Haridon, Lang, Pastuszak & Dobrowolski ( 1978), (d) present paper. (5) 116.4 (6) of L-lysine-PtC16, a favourable interaction of the e-NH~ group with the C1 atoms of the PtCI 2-octahedron is achieved through a similar value of the dihedral angle Z4.…”

Section: (8)mentioning

confidence: 99%

L-Lysine sulphate, C6H16N2O22+.SO42−: a novel conformation of the L-lysine side chain

Capasso¹,

Mattia²,

Mazzarella³

et al. 1983

Acta Crystallogr C

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Abstract. Mr=244.27 , orthorhombic, P212~2~,(1), b=11.536(1), c=16.594(2)A, V= 1066.8 (3)/k 3, Z --4, D x = 1.52, D m =1.52 Mg m -a, 2(Cu Ka) = 1.5418/k, /z(Cu K~t) = 2.82 mm -a, final R = 0.056 for 1110 observed data. The side chain of the L-lysine molecule adopts an unusual folded conformation, which allows specific ion-pair interactions between the sulphate anion and the a-and e-NH~ groups of the same molecule. This conformation might be found in proteins with an N-terminal lysine crystallized from ammonium sulphate solutions.Introduction. With the development of protein crystal-s lography the organization of the solvent on the surface o(l) 0(2) of the protein molecule is receiving increasing attention, o(3) Ions present in the crystallization medium often interact 0(4) 0(5) with the protein, stabilizing specific conformations of o(6) polar side chains. In this context the sulphate ion is of N nz particular interest since a large number of proteins are c crystallized from concentrated ammonium sulphate cA solutions. In this paper we present the structure of ca L-lysine sulphate, where the side chain of the amino acid c6 cD adopts an unusual conformation which allows an ce interaction of the sulphate anion with the charged aand &amino groups of the same molecule.

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