Effect of V2O5 on the Surface and Structural Characteristics of Potassium Lithium Niobate

It has been suggested that materials with interesting and useful bulk non-linear optical properties might result by substituting vanadium, the lightest element in the group V of periodic table, for Nb or Ta atoms along with Li and three oxygens. It is with this motivation that we have been making attempts to grow single crystals of LiNbO3 doped with various concentrations of V2O5. Unfortunately the results obtained on the ceramic samples of this material have not been very encouraging, owing to their hygroscopic nature. However, our attempts to prepare both ceramic and single-crystalline samples of potassium lithium niobate (K3Li2Nb5O15; KLN) doped V2O5 were successful. In this letter we report the preliminary results concerning our studies on the effect of V2O5 doping on the structural as well as topographic features of both ceramic and single-crystalline samples of KLN.

Probing the role of the C-H center dot center dot center dot O hydrogen bond stabilized polypeptide chain reversal at the C-terminus of designed peptide helices. Structural characterization of three decapeptides

The structural characterization in crystals of three designed decapeptides containing a double D-segment at the C-terminus is described. The crystal structures of the peptides Boc-Leu-Aib-Val-Xxx-Leu-Aib-Val- (D)Ala-(D)Leu-Aib-OMe, (Xxx = Gly 2, (D)Ala 3, Aib 4) have been determined and compared with those reported earlier for peptide 1 (Xxx = Ala) and the all L analogue Boc-Leu-Aib-Val-Ala-Leu-Aib-Val-Ala-Leu-Aib-OMe, which yielded a perfect right-handed a-helical structure. Peptides 1 and 2 reveal a right-handed helical segment spanning residues 1 to 7, ending in a Schellman motif with Ala(8) functioning as the terminating residue. Polypeptide chain reversal occurs at residue 9, a novel feature that appears to be the consequence of a C-(HO)-O-... hydrogen bond between residue 4 (CH)-H-alpha and residue 9 CO groups. The structures of peptides 3 and 4, which lack the pro R hydrogen at the C-alpha atom of residue 4, are dramatically different. Peptide 3 adopts a right-handed helical conformation over the 1 to 7 segment. Residues 8 and 9 adopt at conformations forming a C-terminus type I' beta-turn, corresponding to an incipient left-handed twist of the polypeptide chain. In peptide 4, helix termination occurs at Aib(6), with residues 6 to 9 forming a left-handed helix, resulting in a structure that accommodates direct fusion of two helical segments of opposite twist. Peptides 3 and 4 provide examples of chiral residues occurring in the less favored sense of helical twist; (D)Ala(4) in peptide 3 adopts an alpha(R) conformation, while (L)Val(7) in 4 adopts an alpha(L) conformation. The structural comparison of the decapeptides reported here provides evidence for the role of specific C-(HO)-O-... hydrogen bonds in stabilizing chain reversals at helix termini, which may be relevant in aligning contiguous helical and strand segments in polypeptide structures.

Structural synthesis by transformation of binary chains Strukturelle synthese durch umwandlung binaerer ketten

The paper presents a general method of structural synthesis which can be used to derive all possible simple- and multiple-jointed chains of positive, zero or negative degree-of-freedom. In this method all possible chains with N links and F degrees-of-freedom are derived by the transformation of the corresponding “binary chains” with N binary links and F degrees-of-freedom. The method is illustrated by applying to the case of chains with degrees-of-freedom 1,2,0 and −1.

Structural Studies of Analgesics and Their Interactions. V.* The Crystal and Molecular Structure of Metamizol Monohydrate

Metamizol, Na[Ct3H16N3045], C13H16N304S-Na +, a sulphonyl derivative of amidopyrine, is perhaps the most widely used non-narcotic analgetic and antiinflammatory pyrazolone derivative. The monohydrate of the compound crystallizes in the monoclinic space group P2Jc with eight molecules in a unit cell of dimensions a = 9.143 (3), b = 49.50 (2), c = 7.314 (2)/k and fl = 90.9 (1) °. The structure was solved by direct methods and refined to an R value of 0.080 for 4466 observed reflections. The two crystallographically independent molecules in the structure have similar dimensions. The elongated molecules are hydrophobic at one end and hydrophilic at the other with the middle portion partly hydrophobic and partly hydrophilic. The pyrazolone group in the structure has dimensions similar to those found in uncomplexed antipyrine and amidopyrine. The crystal structure can be described as consisting of double layers of metamizol molecules stacked perpendicular to the b axis. The adjacent double layers are separated by a layer of Naions and water molecules.

Structural Investigations on Poly(4-hydroxy-L-proline). 2. Physicochemical Studies

We report experimental studies which confirm our prediction, namely that the ordered structure of poly(hydroxypro1ine) in solution corresponds to a left-handed helical structure with intrachain hydrogen bonds. The CD studies show that the poly(hydroxypro1ine) molecule has essentially the same conformation in aqueous solution and in the film obtained subsequently by evaporation. X-ray diffraction patterns of the sample in this form (B form) have been recorded at different relative humidities. The patterns recorded at relative humidities over 66% can be interpreted in terms of a helical structure with intrachain hydrogen bonds. These results lead us to conclude that the ordered conformation of poly(hydroxypro1ine) in solution is form B and not form A. This offers a simple explanation for the greater stability of the poly(hydroxypro1ine) helix in solution as compared to the poly(pro1ine) form I1 helix and also for the absence of mutarotation for poly(hydroxypro1ine).

Structural Investigations on Poly(4-hydroxy-L-proline). 1. Theoretical Studies

Model building studies on poly(hydroxypro1ine) indicate that in addition to the well-known helical structure of form A, a left-handed helical structure with trans peptide units and with h = 2.86 A and n = 2.67 (i.e., 8 residues in 3 turns) is also possible. In this structure which is shown to be in agreement with X-ray data of the form B in the next paper, the y-hydroxyl group of an (i + 1)th Hyp residue is hydrogen bonded to the carbonyl oxygen of an (i - 1)th residue. The possibility of a structure with cis peptide units is ruled out. It is shown that both forms A and B are equally favorable from considerations of intramolecular energies. Since form B is further stabilized by intrachain hydrogen bonds, we believe that this is likely to be the ordered conformation for poly(hydroxypro1ine) in water.

Structural and functional studies of Bacillus stearothermophilus serine hydroxymethyl transferase: the role of N341, Y60 and F351 in tetrahydrofolate binding.

SHMT (serine hydoxymethyltransferase), a type I pyridoxal 5'-phosphate-dependent enzyme, catalyses the conversion of L-serine and THF (tetrahydrofolate) into glycine and 5,10 -methylene THE SHMT also catalyses several THF-independent side reactions such as cleavage of P-hydroxy amino acids, trans-amination, racemization and decarboxylation. In the present study, the residues Asn(341), Tyr(60) and Phe(351), which are likely to influence THF binding, were mutated to alanine, alanine and glycine respectively, to elucidate the role of these residues in THF-dependent and -independent reactions catalysed by SHMT. The N341A and Y60A bsSHMT (Bacillus stearothermophilus SHMT) mutants were inactive for the THF-dependent activity, while the mutations had no effect on THF-independent activity. However, mutation of Phe(351) to glycine did not have any effect oil either of the activities. The crystal structures of the glycine binary complexes of the mutants showed that N341A bsSHMT forms an external aldimine as in bsSHMT, whereas Y60A and F351G bsSHMTs exist as a Mixture of internal/external aldimine and gem-diamine forms. Crystal structures of all of the three Mutants obtained in the presence of L-allo-threonine were similar to the respective glycine binary complexes. The structure of the ternary complex of F351G bsSHMT with glycine and FTHF (5-formyl THF) showed that the monoglutamate side chain of FTHF is ordered in both the subunits of the asymmetric unit, unlike in the wild-type bsSHMT. The present studies demonstrate that the residues Asn(341) and Tyr(60) are pivotal for the binding of THF/FTHF, whereas Phe(351) is responsible for the asymmetric binding of FTHF in the two subunits of the dimer.

Synthesis, spectral and structural studies on metal complexes of Schiff bases involving vitamin B6 and histamine

Six metal complexes of Schiff bases involving Vitamin B6 and the decarboxylated amino acid histamine have been synthesised and characterized. Crystal structures have been determined for [CuL1(H2O)Br]-NO31(L1= pyridoxylidenehistamine) and [Cu2L22(NO3)2]·6H2O 2(L2= 5′-phosphopyridoxylidenehistaminate). The crystal structure of complex 1[space group P[1 with combining macron], a= 8.161(2), b= 10.368(2), c= 11.110(2)Å, α= 105.18(1), β= 102.12(1), γ= 72.10(1)° and Z= 2; R= 0.072, R′= 0.083] consists of square-pyramidally co-ordinated copper with the tridentate Schiff base in the zwitterionic form, whereas in 2[space group P[1 with combining macron], a= 8.727(1), b= 10.308(1), c= 12.845(2)Å, α= 110.00(1), β= 78.94(1), γ= 114.35(1)° and Z= 1; R= 0.035, R′= 0.034] the copper has the same co-ordination geometry but the tetradentate Schiff-base ligand exists as a monoanion. The conformational parameters deduced from such structures are important for understanding the stereochemical aspects of Vitamin B6-catalysed model reactions involving histidine.

Synthetic, spectroscopic, magnetic, and x-ray structural studies on a vitamin B6-amino acid Schiff base complex, aqua(5'-phosphopyridoxylidenetyrosinato)copper(II) tetrahydrate

A Schiff base metal complex, [Cu(II)(PLP-DL-tyrosinato)(H2O)].4H2O (PLP = pyridoxal phosphate), with the molecular formula CuC17O13N2H27P has been prepared and characterized by magnetic, spectral, and X-ray structural studies. The compound crystallizes in the triclinic space group P1BAR with a = 8.616 (2) angstrom, b = 11.843 (3) angstrom, c = 12.177 (3) angstrom, alpha = 103.40 (2)degrees, beta = 112.32 (2)degrees, gamma = 76.50 (1)degrees, and Z = 2. The structure was solved by the heavy-atom method and refined by least-squares techniques to a final R value of 0.057 for 3132 independent reflections. The coordination geometry around Cu(II) is distorted square pyramidal with phenolic oxygen, imino nitrogen, and carboxylate oxygen from the Schiff base ligand and water oxygen as basal donor atoms. The axial site is occupied by a phosphate oxygen from a neighboring molecule, thus resulting in a one-dimensional polymer. The structure reveals pi-pi interaction of the aromatic side chain of the amino acid with the pyridoxal pi system. A comparative study is made of this complex with similar Schiff base complexes. The variable-temperature magnetic behavior of this compound shows a weak antiferromagnetic interaction.

Biochemical and structural characterization of recombinant hyoscyamine 6 beta-hydroxylase from Datura metel L.

Hyoscyamine 6 beta-hydroxylase (H6H; EC 1.14.11.11), an important enzyme in the biosynthesis of tropane alkaloids, catalyzes the hydroxylation of hyoscyamine to give 6 beta-hydroxyhyoscyamine and its epoxidation in the biosynthetic pathway leading to scopolamine. Datura metel produces scopolamine as the predominant tropane alkaloid. The cDNA encoding H6H from D. mete! (DmH6H) was cloned, heterologously expressed and biochemically characterized. The purified recombinant His-tagged H6H from D. mete! (DmrH6H) was capable of converting hyoscyamine to scopolamine. The functionally expressed DmrH6H was confirmed by HPLC and ESI-MS verification of the products, 6 beta-hydroxyhyoscyamine and its derivative, scopolamine; the DmrH6H epoxidase activity was low compared to the hydroxylase activity. The K-m values for both the substrates, hyoscyamine and 2-oxoglutarate, were 50 mu M each. The CD (circular dichroism) spectrum of the DmrH6H indicated a preponderance of alpha-helicity in the secondary structure. From the fluorescence studies, Stern-Volmer constants for hyoscyamine and 2-oxoglutarate were found to be 0.14 M-1 and 0.56 M-1, respectively. These data suggested that the binding of the substrates, hyoscyamine and 2-oxoglutarate, to the enzyme induced significant conformational changes. (C) 2010 Elsevier Masson SAS. All rights reserved.

Deformation and structural densification in Al2O3-Y2O3 glass

In this article, we examine the unusual plastic deformation under uniaxial compression of an Al2O3-15 mol % Y2O3 (A15Y) glass synthesized by a wet chemical route At a low temperature of 650-725 degrees C, plastic deformation of this glass is largely non-viscous through shear instabilities In contrast deformation near the crystallization temperature (850 degrees C) occurs homogeneously with work hardening and with a monotonic increase in the true density of the glass by 10-12% accompanied by an increase in hardness (H) and elastic modulus (E) of up to 100% We hypothesize a phenomenon of molecular densification of the amorphous structure through a hierarchy of multiple phases, analogous to density- or entropy-driven amorphous to-amorphous phase transitions (polyamorphism) These results suggest that the present method of preparation and the unusual behavior can trigger a search for many more systems that display such behavior (C) 2010 Acta Materialia Inc Published by Elsevier Ltd All rights reserved