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

Abstract

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.

A molecular orbital study of C–H···Cl– and N–H···Cl– hydrogen bonds. Inferences on selected metal complexes and on protein ClC Cl– channels

“…The computed C-N and N-H bond distances are 1.516 and 1.026 Å at B3LYP/6-31+G** and 1.507 and 1.023 Å at MP2/6-31+G**, respectively. The computed values agree excellently with those found at the solid state for L-lysine sulfate [45].…”

Structure of a calcium-deficient form of influenza virus neuraminidase: implications for substrate binding

“…Lying close to Asp151, but outside the substrate-binding site, is a second sulfate anion that forms a hydrogen bond with the N 1 atom of His150 (SBS2). The distance of closest approach between the carboxylate O atom of the side chain of Asp151 and an O atom of this sulfate falls in the range 2.71-3.41 Å in the four monomers; these distances are consistent with a neutral carboxyl group (Vilminot et al, 1974;Cano & Martínez-Carrera, 1974;Vilminot & Philippot, 1976;Capasso et al, 1983;Nagashima et al, 1992;Srinivasan et al, 2001a,b). Sequence analysis of clinical isolates of influenza virus have identified Asp151 as the most variable of the conserved residues (McKimm-Breschkin et al, 2003); substitution by residues incapable of acting as an acid (asparagine, valine and glycine), however, deny Asp151 a critical role in catalysis.…”

Crystal Structure and Physicochemical Properties of 2-Diisopropylammonium Ethylammonium Sulfate Dihydrate

“…(1) 109.84 (7) 110.43 (7) 108.73 (8) (2) and O(4) each engaged in two hydrogen bonds have longer distances. The high sensitivity of the S-O bond distances to the strength and the number of the hydrogen bonds which may be formed, has been also noted in other crystal structures [13][14][15]. The calculated values of the distortion indices corresponding to the different distances and angles in the tetrahedron are: DI(SO) = 0.0034; DI(OO) = 0.0026; DI(OSO)) = 0.004 [16].…”