Home About us Contact
|
Home About us Contact | ||
|
|
||
Structure Shows (structure + shows)
Selected AbstractsStructural Characterization and a New One-Pot Synthesis of trans -Chloro(phenyl)bis(triphenylphosphane)nickel(II)EUROPEAN JOURNAL OF INORGANIC CHEMISTRY, Issue 9 2003Alexander Zeller Abstract trans -[NiCl(Ph)(PPh3)2], the organometallic precursor for a new class of neutral polymerization catalysts, has been synthesized via a new synthetic route. The previously used alkylaluminum compounds are replaced by zinc dust for the reduction of the nickel(II) salt in the presence of triphenylphosphane forming the intermediate Ni(PPh3)4. In a one-pot reaction, chlorobenzene then adds oxidatively to the intermediate to form the title compound, which was structurally characterized, in high yields. Its geometry is compared to known structures of the higher homologues of group 10. All complexes adopt a distorted square-planar geometry, but the parent structure shows significantly shorter metal-ligand bond lengths than its Pd and Pt congeners, as expected. Density functional theory calculations (B3LYP/6,31G*) on the full structure are in very good agreement with the solid-state structure. (© Wiley-VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2003) [source] Solid-State Structure and Tautomerism of 2-Aminotroponimines Studied by X-ray Crystallography and Multinuclear NMR SpectroscopyEUROPEAN JOURNAL OF ORGANIC CHEMISTRY, Issue 21 2004Rosa M. Claramunt Abstract Structural studies in the solid state by X-ray crystallography and by 13C and 15N CPMAS NMR spectroscopy carried out on a series of 2-aminotroponimine derivatives 2,5 has allowed to establish the existence of hydrogen bonding and to determine the most stable tautomer. Almost all the structures reflect the classical double-well potential function for the N,H···N hydrogen bonds. Only in the case of the compound N -(pyrrol-1-yl)-2-(pyrrol-1-ylamino)troponimine (5) the crystal structure shows two independent molecules, one with a classical hydrogen bond and another with either a single-well or a low-barrier hydrogen bond. The structure of this compound is discussed with the use of the solid-state NMR spectroscopic data. 2-Aminotropones, as intermediates to the 2-aminotroponimines, show the oxo-tautomer as the stable form. B3LYP/6-31G* calculations are used to rationalise the experimental results. (© Wiley-VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2004) [source] Solution structure of the functional domain of Paracoccus denitrificans cytochrome c552 in the reduced stateFEBS JOURNAL, Issue 13 2000Primo, Pristov In order to determine the solution structure of Paracoccus denitrificans cytochrome c552 by NMR, we cloned and isotopically labeled a 10.5-kDa soluble fragment (100 residues) containing the functional domain of the 18.2-kDa membrane-bound protein. Using uniformly 15N-enriched samples of cytochrome c552 in the reduced state, a variety of two-dimensional and three-dimensional heteronuclear double-resonance NMR experiments was employed to achieve complete 1H and 15N assignments. A total of 1893 distance restraints was derived from homonuclear 2D-NOESY and heteronuclear 3D-NOESY spectra; 1486 meaningful restraints were used in the structure calculations. After restrained energy minimization a family of 20 structures was obtained with rmsd values of 0.56 ± 0.10 Å and 1.09 ± 0.09 Å for the backbone and heavy atoms, respectively. The overall topology is similar to that seen in previously reported models of this class of proteins. The global fold consists of two long helices at the N-terminus and C-terminus and three shorter helices surrounding the heme moiety; the helices are connected by well-defined loops. Comparison with the X-ray structure shows some minor differences in the positions of the Trp57 and Phe65 side-chain rings as well as the heme propionate groups. [source] Mammals in South American drylands: faunal similarity and trophic structureGLOBAL ECOLOGY, Issue 2 2000Ricardo A. Ojeda Abstract We compared the fauna of small mammals (less than 500 g body weight) among five major South American drylands (Atacama, Altiplano, Monte, Patagonia and Caatinga) and found considerable heterogeneity and distinctiveness in species richness and composition between these biomes. From a total of 89 recorded species, 76 of them are restricted to only one of these drylands. The highland desert, or Altiplano, is the biome with the highest number of species. Despite the marked differences in the composition of the mammalian fauna, the trophic structure shows a rather consistent pattern: herbivores are the most important trophic group in all drylands. This consistency seems to be more the result of phylogenetic inertia than of similar ecological processes. Our results are compared with recent studies on desert small mammals across continents. [source] Electronically controlled multiphase sinusoidal oscillators using current amplifiersINTERNATIONAL JOURNAL OF CIRCUIT THEORY AND APPLICATIONS, Issue 1 2009George Souliotis Abstract A novel current-mode multiphase oscillator topology is introduced in this letter. This is realized by employing current amplifiers and only grounded capacitors. Attractive characteristics offered by the new topology are the electronic adjustment of the oscillation frequency, the absence of passive resistors, and the requirement of only grounded capacitors. Comparison with the corresponding already published current follower based structure shows that the proposed topology has better performance in terms of the number of required active elements, the employment of passive resistors, and the ability for electronic adjustment of the oscillation frequency. Copyright © 2008 John Wiley & Sons, Ltd. [source] A visualized analysis of small-angle neutron scattering intensity: concentration fluctuation in alcohol,water mixturesJOURNAL OF APPLIED CRYSTALLOGRAPHY, Issue 2007T. Sato Small-angle neutron scattering measurements have been performed on tert -butyl alcohol,water mixtures with alcohol concentrations from 0.05 to 0.30 mole fractions at 298, 313 and 328,K. Concentration fluctuations of the mixtures are analysed in terms of fractals. The structure of the concentration fluctuation is visualized by means of a large-scale reverse Monte Carlo technique. Percolation analysis of the visualized structure shows that the concentration fluctuation is characterized by polydisperse mass fractals, as found for 1-propanol,water mixtures. It seems that polydisperse mass fractals are a common structural characteristic in various alcohol,water mixtures. [source] Collagen structure: The molecular source of the tendon magic angle effectJOURNAL OF MAGNETIC RESONANCE IMAGING, Issue 2 2007Gary D. Fullerton PhD Abstract This review of tendon/collagen structure shows that the orientational variation in MRI signals from tendon, which is referred to as the "magic angle" (MA) effect, is caused by irreducible separation of charges on the main chain of the collagen molecule. These charges are held apart in a vacuum by stereotactic restriction of protein folding due in large part to a high concentration of hydroxyproline ring residues in the amino acids of mammalian collagen. The elevated protein electrostatic energy is reduced in water by the large dielectric constant of the highly polar solvent (, , 80). The water molecules serve as dielectric molecules that are bound by an energy that is nearly equivalent to the electrostatic energy between the neighboring positive and negative charge pairs in a vacuum. These highly immobilized water molecules and secondary molecules in the hydrogen-bonded water network are confined to the transverse plane of the tendon. Orientational restriction causes residual dipole coupling, which is directly responsible for the frequency and phase shifts observed in orientational MRI (OMRI) described by the MA effect. Reference to a wide range of biophysical measurements shows that native hydration is a monolayer on collagen hm = 1.6 g/g, which divides into two components consisting of primary hydration on polar surfaces hpp = 0.8 g/g and secondary hydration hs = 0.8 g/g bridging over hydrophobic surface regions. Primary hydration further divides into side-chain hydration hpsc = 0.54 g/g and main-chain hydration hpmc = 0.263 g/g. The main-chain fraction consists of water that bridges between charges on the main chain and is responsible for almost all of the enthalpy of melting ,H = 70 J/g-dry mass. Main-chain water bridges consist of one extremely immobilized Ramachandran water bridge per tripeptide hRa = 0.0658 g/g and one double water bridge per tripeptide hdwb = 0.1974 g/g, with three water molecules that are sufficiently slowed to act as the spin-lattice relaxation sink for the entire tendon. J. Magn. Reson. Imaging 2007. © 2007 Wiley-Liss, Inc. [source] Low- P,high- T metamorphism and the role of heat transport by melt migration in the Higo Metamorphic Complex, Kyushu, JapanJOURNAL OF METAMORPHIC GEOLOGY, Issue 9 2004K. MIYAZAKIArticle first published online: 7 JAN 200 Abstract This paper characterizes the metamorphic thermal structure of the Higo Metamorphic Complex (HMC) and presents the results of a numerical simulation of a geotherm with melt migration and solidification. Reconstruction of the geological and metamorphic structure shows that the HMC initially had a simple thermal structure where metamorphic temperatures and pressures increased towards apparent lower structural levels. Subsequently, this initial thermal structure has been collapsed by E,W and NNE,SSW trending high-angle faults. Pressure and temperature conditions using the analysis of mineral assemblages and thermobarometry define a metamorphic field P,T array that may be divided into two segments: the array at apparent higher structural levels has a low-dP/dT slope, whereas that at apparent lower structural levels has a high-dP/dT slope. This composite array cannot be explained by heat conduction in subsolidus rocks alone. Migmatite is exposed pervasively at apparent lower structural levels, but large syn-metamorphic plutons are absent at the levels exposed in the HMC. Transport and solidification of melt within migmatite is a potential mechanism to generate the composite array. Thermal modelling of a geotherm with melt migration and solidification shows that the composite thermal structure may be formed by a change of the dominant heat transfer from an advective regime to a conduction regime with decreasing depth. The model also predicts that strata beneath the crossing point will consist of high-grade solid metamorphic rocks and solidified melt products, such as migmatite. This prediction is consistent with the observation that migmatite was associated with the very high-dP/dT slope. The melt migration model is able to generate the very high-dP/dT segment due to the high rate of heat transfer by advection. [source] Cathodoluminescence, High-Resolution X-Ray Diffraction and Transmission-Electron-Microscopy Investigations of Cubic AlGaN/GaN Quantum WellsPHYSICA STATUS SOLIDI (C) - CURRENT TOPICS IN SOLID STATE PHYSICS, Issue 1 2003D.J. As Abstract The structural and optical properties of cubic Al0.25Ga0.75N/GaN multi quantum well structures grown on GaAs (001) substrates by radio-frequency plasma-assisted molecular beam epitaxy (MBE) are reported. Transmission electron microscopy (TEM), high resolution X-ray diffraction (HRXRD), and cathodoluminescence (CL) measurements are used to characterize the cubic Al0.25Ga0.75N/GaN quantum wells. The interfaces between the quantum-well and barrier layers are well resolved, abrupt and the entire structure shows an excellent periodicity. Due to the high dislocation density of about 1010 cm,2 a severe broadening of the XRD-reflection is observed and superlattice satellite peaks are only weakly indicated. Further, a wavy structure is seen in TEM at the coalescence of submicron-size grains. Nevertheless, CL at room temperature shows a strong emission of quantized states at 3.352 eV. [source] Degradation of Structural and Optical Properties of InGaN/GaN Multiple Quantum Wells with Increasing Number of WellsPHYSICA STATUS SOLIDI (C) - CURRENT TOPICS IN SOLID STATE PHYSICS, Issue 1 2003S. Pereira Abstract We compare the structural and spectral properties of two multi quantum wells (MQWs), grown by metal organic chemical vapour deposition under the same nominal conditions, with a different number of periods. The MQWs, each with 20% InN and containing 8 and 18 wells, respectively, grew on-axis and coherent to GaN, as revealed by X-ray diffraction reciprocal space mapping (RSM) analysis. Comparison of the asymmetrical (105) RSMs indicates an overall structural deterioration and greater well-barrier intermixing for the MQW with the larger number of wells. Moreover, the composition of the MQWs was depth-profiled by grazing incidence Rutherford backscattering spectrometry (RBS). RBS further evidences strong intermixing in the 18-well heterostructure. The deleterious effects of intermixing on the emission spectrum are revealed by low temperature photoluminescence spectroscopy. Despite similar peak emission energies (,E < 45 meV) the 8-well structure shows a more symmetric and narrow peak (FWHM , 100 meV) in comparison with that of the 18-well sample (FWHM , 170 meV). Surface analyses by atomic force and scanning electron microscopy show an increased density, size and depth of V-pit defects on the 18-well structure. These results suggest that dislocations and pitting result from a larger elastic strain energy accumulated in the thicker MQW stack and are a fundamental intermixing mechanism for InGaN/GaN MQWs. [source] Magnetic behaviour of synthetic Co2SiO4ACTA CRYSTALLOGRAPHICA SECTION B, Issue 6 2009Andrew Sazonov Synthetic Co2SiO4 crystallizes in the olivine structure (space group ) with two crystallographically non-equivalent Co positions and shows antiferromagnetic ordering below 50,K. We have investigated the temperature variation of the Co2SiO4 magnetic structure by means of non-polarized and polarized neutron diffraction for single crystals. Measurements with non-polarized neutrons were made at 2.5,K (below TN), whereas polarized neutron diffraction experiments were carried out at 70 and 150,K (above TN) in an external magnetic field of 7,T parallel to the b axis. Additional accurate non-polarized powder diffraction studies were performed in a broad temperature range from 5 to 500,K with small temperature increments. Detailed symmetry analysis of the Co2SiO4 magnetic structure shows that it corresponds to the magnetic (Shubnikov) group Pnma, which allows the antiferromagnetic configuration (Gx, Cy, Az) for the 4a site with inversion symmetry (Co1 position) and (0,Cy,0) for the 4c site with mirror symmetry m (Co2 position). The temperature dependence of the Co1 and Co2 magnetic moments obtained from neutron diffraction experiments was fitted in a modified molecular-field model. The polarized neutron study of the magnetization induced by an applied field shows a non-negligible amount of magnetic moment on the oxygen positions, indicating a delocalization of the magnetic moment from Co towards neighbouring O owing to superexchange coupling. The relative strength of the exchange interactions is discussed based on the non-polarized and polarized neutron data. [source] Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomeraseACTA CRYSTALLOGRAPHICA SECTION D, Issue 8 2010Mikko Salin Crystallographic binding studies have been carried out to probe the active-site binding properties of a monomeric variant (A-TIM) of triosephosphate isomerase (TIM). These binding studies are part of a structure-based directed-evolution project aimed towards changing the substrate specificity of monomeric TIM and are therefore aimed at finding binders which are substrate-like molecules. A-TIM has a modified more extended binding pocket between loop-7 and loop-8 compared with wild-type TIM. The A-TIM crystals were grown in the presence of citrate, which is bound in the active site of each of the two molecules in the asymmetric unit. In this complex, the active-site loops loop-6 and loop-7 adopt the closed conformation, similar to that observed in liganded wild-type TIM. Extensive crystal-soaking protocols have been developed to flush the bound citrate out of the active-site pocket of both molecules and the crystal structure shows that the unliganded open conformation of the A-TIM active site is the same as in unliganded wild-type TIM. It is also shown that sulfonate compounds corresponding to the transition-state analogue 2-phosphoglycolate bind in the active site, which has a closed conformation. It is also shown that the new binding pocket of A-TIM can bind 3-phosphoglycerate (3PGA; an analogue of a C4-sugar phosphate) and 4-phospho- d -erythronohydroxamic acid (4PEH; an analogue of a C5-sugar phosphate). Therefore, these studies have provided a rationale for starting directed-evolution experiments aimed at generating the catalytic properties of a C5-sugar phosphate isomerase on the A-TIM framework. [source] Structure of endoglucanase Cel9A from the thermoacidophilic Alicyclobacillus acidocaldariusACTA CRYSTALLOGRAPHICA SECTION D, Issue 8 2009Jose Henrique Pereira The production of biofuels using biomass is an alternative route to support the growing global demand for energy and to also reduce the environmental problems caused by the burning of fossil fuels. Cellulases are likely to play an important role in the degradation of biomass and the production of sugars for subsequent fermentation to fuel. Here, the crystal structure of an endoglucanase, Cel9A, from Alicyclobacillus acidocaldarius (Aa_Cel9A) is reported which displays a modular architecture composed of an N-terminal Ig-like domain connected to the catalytic domain. This paper describes the overall structure and the detailed contacts between the two modules. Analysis suggests that the interaction involving the residues Gln13 (from the Ig-like module) and Phe439 (from the catalytic module) is important in maintaining the correct conformation of the catalytic module required for protein activity. Moreover, the Aa_Cel9A structure shows three metal-binding sites that are associated with the thermostability and/or substrate affinity of the enzyme. [source] Structures and molecular-dynamics studies of three active-site mutants of bovine pancreatic phospholipase A2ACTA CRYSTALLOGRAPHICA SECTION D, Issue 10 2008Shankar Prasad Kanaujia Phospholipase A2 hydrolyzes phospholipids at the sn -2 position to cleave the fatty-acid ester bond of l -glycerophospholipids. The catalytic dyad (Asp99 and His48) along with a nucleophilic water molecule is responsible for enzyme hydrolysis. Furthermore, the residue Asp49 in the calcium-binding loop is essential for controlling the binding of the calcium ion and the catalytic action of phospholipase A2. To elucidate the structural role of His48 and Asp49, the crystal structures of three active-site single mutants H48N, D49N and D49K have been determined at 1.9,Å resolution. Although the catalytically important calcium ion is present in the H48N mutant, the crystal structure shows that proton transfer is not possible from the catalytic water to the mutated residue. In the case of the Asp49 mutants, no calcium ion was found in the active site. However, the tertiary structures of the three active-site mutants are similar to that of the trigonal recombinant enzyme. Molecular-dynamics simulation studies provide a good explanation for the crystallographic results. [source] Structure of the mexicain,E-64 complex and comparison with other cysteine proteases of the papain familyACTA CRYSTALLOGRAPHICA SECTION D, Issue 5 2007J. A. Gavira Mexicain is a 23.8,kDa cysteine protease from the tropical plant Jacaratia mexicana. It is isolated as the most abundant product after cation-exchange chromatography of the mix of proteases extracted from the latex of the fruit. The purified enzyme inhibited with E-64 [N -(3-carboxyoxirane-2-carbonyl)-leucyl-amino(4-guanido)butane] was crystallized by sitting-drop vapour diffusion and the structure was solved by molecular replacement at 2.1,Å resolution and refined to an R factor of 17.7% (Rfree = 23.8%). The enzyme belongs to the ,+, class of proteins and the structure shows the typical papain-like fold composed of two domains, the ,-helix-rich (L) domain and the ,-barrel-like (R) domain, separated by a groove containing the active site formed by residues Cys25 and His159, one from each domain. The four monomers in the asymmetric unit show one E-64 molecule covalently bound to Cys25 in the active site and differences have been found in the placement of E-64 in each monomer. [source] Structural flexibility, an essential component of the allosteric activation in Escherichia coli glucosamine-6-phosphate deaminaseACTA CRYSTALLOGRAPHICA SECTION D, Issue 1 2002E. Rudiño-Piñera A new crystallographic structure of the free active-site R conformer of the allosteric enzyme glucosamine-6-phosphate deaminase from Escherichia coli, coupled with previously reported structures of the T and R conformers, generates a detailed description of the heterotropic allosteric transition in which structural flexibility plays a central role. The T conformer's external zone [Horjales et al. (1999), Structure, 7, 527,536] presents higher B values than in the R conformers. The ligand-free enzyme (T conformer) undergoes an allosteric transition to the free active-site R conformer upon binding of the allosteric activator. This structure shows three alternate conformations of the mobile section of the active-site lid (residues 163,182), in comparison to the high B values for the unique conformation of the T conformer. One of these alternate R conformations corresponds to the active-site lid found when the substrate is bound. The disorder associated with the three alternate conformations can be related to the biological regulation of the Km of the enzyme for the reaction, which is metabolically required to maintain adequate concentrations of the activator, which holds the enzyme in its R state. Seven alternate conformations for the active-site lid and three for the C-terminus were refined for the T structure using isotropic B factors. Some of these conformers approach that of the R conformer in geometry. Furthermore, the direction of the atomic vibrations obtained with anisotropic B refinement supports the hypothesis of an oscillating rather than a tense T state. The concerted character of the allosteric transition is also analysed in view of the apparent dynamics of the conformers. [source] The structure of human aldose reductase bound to the inhibitor IDD384ACTA CRYSTALLOGRAPHICA SECTION D, Issue 5 2000Vito Calderone The crystallographic structure of the complex between human aldose reductase (AR2) and one of its inhibitors, IDD384, has been solved at 1.7,Å resolution from crystals obtained at pH 5.0. This structure shows that the binding of the inhibitor's hydrophilic head to the catalytic residues Tyr48 and His110 differs from that found previously with porcine AR2. The difference is attributed to a change in the protonation state of the inhibitor (pKa = 4.52) when soaked with crystals of human (at pH 5.0) or pig lens AR2 (at pH 6.2). This work demonstrates how strongly the detailed binding of the inhibitor's polar head depends on its protonation state. [source] Expression, purification, crystallization and structure of human adipocyte lipid-binding protein (aP2)ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 11 2006Eric Marr Human adipocyte lipid-binding protein (aP2) belongs to a family of intracellular lipid-binding proteins involved in the transport and storage of lipids. Here, the crystal structure of human aP2 with a bound palmitate is described at 1.5,Å resolution. Unlike the known crystal structure of murine aP2 in complex with palmitate, this structure shows that the fatty acid is in a folded conformation and that the loop containing Phe57 acts as a lid to regulate ligand binding by excluding solvent exposure to the central binding cavity. [source] Structure of Staphylococcus aureus guanylate monophosphate kinaseACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 10 2006Kamel El Omari Nucleotide monophosphate kinases (NMPKs) are potential antimicrobial drug targets owing to their role in supplying DNA and RNA precursors. The present work reports the crystal structure of Staphylococcus aureus guanylate monophosphate kinase (SaGMK) at 1.9,Å resolution. The structure shows that unlike most GMKs SaGMK is dimeric, confirming the role of the extended C-terminus in dimer formation as first observed for Escherichia coli GMK (EcGMK). One of the two SaGMK dimers within the crystal asymmetric unit has two monomers in different conformations: an open form with a bound sulfate ion (mimicking the ,-phosphate of ATP) and a closed form with bound GMP and sulfate ion. GMP-induced domain movements in SaGMK can thus be defined by comparison of these conformational states. Like other GMKs, the binding of GMP firstly triggers a partial closure of the enzyme, diminishing the distance between the GMP-binding and ATP-binding sites. In addition, the closed structure shows the presence of a potassium ion in contact with the guanine ring of GMP. The potassium ion appears to form an integral part of the GMP-binding site, as the Tyr36 side chain has significantly moved to form a metal ion,ligand coordination involving the lone pair of the side-chain O atom. The potassium-binding site might also be exploited in the design of novel inhibitors. [source] Solution Structure of a DNA Duplex Containing a Biphenyl PairCHEMISTRY - A EUROPEAN JOURNAL, Issue 4 2008Zeena Johar Abstract Hydrogen-bonding and stacking interactions between nucleobases are considered to be the major noncovalent interactions that stabilize the DNA and RNA double helices. In recent work we found that one or multiple biphenyl pairs, devoid of any potential for hydrogen bond formation, can be introduced into a DNA double helix without loss of duplex stability. We hypothesized that interstrand stacking interactions of the biphenyl residues maintain duplex stability. Here we present an NMR structure of the decamer duplex d(GTGACXGCAG), d(CTGCYGTCAC) that contains one such X/Y biaryl pair. X represents a 3,,,5,,-dinitrobiphenyl- and Y a 3,,,4,,-dimethoxybiphenyl C -nucleoside unit. The experimentally determined solution structure shows a B-DNA duplex with a slight kink at the site of modification. The biphenyl groups are intercalated side by side as a pair between the natural base pairs and are stacked head to tail in van der Waals contact with each other. The first phenyl rings of the biphenyl units each show tight intrastrand stacking to their natural base neighbors on the 3,-side, thus strongly favoring one of two possible interstrand intercalation structures. In order to accommodate the biphenyl units in the duplex the helical pitch is widened while the helical twist at the site of modification is reduced. Interestingly, the biphenyl rings are not static in the duplex but are in dynamic motion even at 294,K. [source] The calpain 1,,-actinin interactionFEBS JOURNAL, Issue 23 2003Resting complex between the calcium-dependant protease, its target in cytoskeleton Calpain 1 behaviour toward cytoskeletal targets was investigated using two ,-actinin isoforms from smooth and skeletal muscles. These two isoforms which are, respectively, sensitive and resistant to calpain cleavage, interact with the protease when using in vitro binding assays. The stability of the complexes in EGTA [Kd(,Ca2+) = 0.5 ± 0.1 µm] was improved in the presence of 1 mm calcium ions [Kd(+Ca2+) = 0.05 ± 0.01 µm]. Location of the binding structures shows that the C-terminal domain of ,-actinin and each calpain subunit, 28 and 80 kDa, participates in the interaction. In particular, the autolysed calpain form (76/18) affords a similar binding compared to the 80/28 intact enzyme, with an identified binding site in the catalytic subunit, located in the C-terminal region of the chain (domain III,IV). The in vivo colocalization of calpain 1 and ,-actinin was shown to be likely in the presence of calcium, when permeabilized muscle fibres were supplemented by exogenous calpain 1 and the presence of calpain 1 in Z-line cores was shown by gold-labelled antibodies. The demonstration of such a colocalization was brought by coimmunoprecipitation experiments of calpain 1 and ,-actinin from C2.7 myogenic cells. We propose that calpain 1 interacts in a resting state with cytoskeletal targets, and that this binding is strengthened in pathological conditions, such as ischaemia and dystrophies, associated with high calcium concentrations. [source] Three-dimensional structure of the histidine-containing phosphocarrier protein (HPr) from Enterococcus faecalis in solutionFEBS JOURNAL, Issue 3 2001Till Maurer The histidine-containing phosphocarrier protein (HPr) transfers a phosphate group between components of the prokaryotic phosphoenolpyruvate-dependent phosphotransferase system (PTS), which is finally used to phosphorylate the carbohydrate transported by the PTS through the cell membrane. Recently it has also been found to act as an intermediate in the signaling cascade that regulates transcription of genes related to the carbohydrate-response system. Both functions involve phosphorylation/dephosphorylation reactions, but at different sites. Using multidimensional 1H-NMR spectroscopy and angular space simulated annealing calculations, we determined the structure of HPr from Enterococcus faecalis in aqueous solution using 1469 distance and 44 angle constraints derived from homonuclear NMR data. It has a similar overall fold to that found in HPrs from other organisms. Four , strands, A, B, C, D, encompassing residues 2,7, 32,37, 40,42 and 60,66, form an antiparallel , sheet lying opposite the two antiparallel , helices, a and c (residues 16,26 and 70,83). A short , helix, b, from residues 47,53 is also observed. The pairwise root mean square displacement for the backbone heavy atoms of the mean of the 16 NMR structures to the crystal structure is 0.164 nm. In contrast with the crystalline state, in which a torsion angle strain in the active-center loop has been described [Jia, Z., Vandonselaar, M., Quail, J.W. & Delbaere, L.T.J. (1993) Nature (London) 361, 94,97], in the solution structure, the active-site His15 rests on top of helix a, and the phosphorylation site N,1 of the histidine ring is oriented towards the surface, making it easily accessible to the solvent. Back calculation of the 2D NOESY NMR spectra from both the NMR and X-ray structures shows that the active-center structure derived by X-ray crystallography is not compatible with experimental data recorded in solution. The observed torsional strain must either be a crystallization artefact or represents a conformational state that exists only to a small extent in solution. [source] Palladium(II) Complexes of C2 -Bridged Chiral Diphosphines: Application to Enantioselective Carbonyl-Ene ReactionsADVANCED SYNTHESIS & CATALYSIS (PREVIOUSLY: JOURNAL FUER PRAKTISCHE CHEMIE), Issue 8 2010He-Kuan Luo Abstract (11bR,11,bR)-4,4,-(1,2-Phenylene)bis[4,5-dihydro-3H -dinaphtho[2,1- c:1,,2,- e]phosphepin] [abbreviated as (R)-BINAPHANE], (3R,3,R,4S,4,S,11bS,11,bS)-4,4,-bis(1,1-dimethylethyl)-4,4,,5,5,-tetrahydro-3,3,-bi-3H -dinaphtho[2,1- c:1,,2,- e]phosphepin [(S)-BINAPINE], (1S,1,S,2R,2,R)-1,1,-bis(1,1-dimethylethyl)-2,2,-biphospholane [(S,S,R,R)-TANGPHOS] and (2R,2,R,5R,5,R)-1,1,-(1,2-phenylene)bis[2,5-bis(1-methylethyl)phospholane] [(R,R) -i- Pr-DUPHOS] are C2 -bridged chiral diphosphines that form stable complexes with palladium(II) and platinum(II) containing a five-membered chelate ring. The Pd(II)-BINAPHANE catalyst displayed good to excellent enantioselectivities with ee values as high as 99.0% albeit in low yields for the carbonyl-ene reaction between phenylglyoxal and alkenes. Its Pt(II) counterpart afforded improved yields while retaining satisfactory enantioselectivity. For the carbonyl-ene reaction between ethyl trifluoropyruvate and alkenes, the Pd(II)-BINAPHANE catalyst afforded both good yields and extremely high enantioselectivities with ees as high as 99.6%. A comparative study on the Pd(II) catalysts of the four C2 -bridged chiral diphosphines revealed that Pd(II)-BINAPHANE afforded the best enantioselectivity. The ee values derived from Pd(II)-BINAPHANE are much higher than those derived from the other three Pd(II) catalysts. A comparison of the catalyst structures shows that the Pd(II)-BINAPHANE catalyst is the only one that has two bulky (R)-binaphthyl groups close to the reaction site. Hence it creates a deep chiral space that can efficiently control the reaction behavior in the carbonyl-ene reactions resulting in excellent enantioselectivity. [source] Super-Hydrophobic PDMS Surface with Ultra-Low Adhesive Force,MACROMOLECULAR RAPID COMMUNICATIONS, Issue 22 2005Meihua Jin Abstract Summary: Rough polydimethylsiloxane (PDMS) surface containing micro-, submicro- and nano-composite structures was fabricated using a facile one-step laser etching method. Such surface shows a super-hydrophobic character with contact angle higher than 160° and sliding angle lower than 5°, i.e. self-cleaning effect like lotus leaf. The wettabilities of the rough PDMS surfaces can be tunable by simply controlling the size of etched microstructures. The adhesive force between etched PDMS surface and water droplet is evaluated, and the structure effect is deduced by comparing it with those own a single nano- or micro-scale structures. This super-hydrophobic PDMS surface can be widely applied to many areas such as liquid transportation without loss, and micro-pump (creating pushing-force) needless micro-fluidic devices. Etched PDMS surface containing micro-, submicro-, and nano-composite structures shows a self-cleaning effect with water CA as high as 162° and SA lower than 5°. [source] Effect of stack number on the threshold current density and emission wavelength in quantum dash/dot lasersPHYSICA STATUS SOLIDI (C) - CURRENT TOPICS IN SOLID STATE PHYSICS, Issue 10 2009D. Zhou Abstract InAs quantum dash and dot (QDH and QD) lasers grown by molecular beam epitaxy on InP substrate are studied. The grown lasers with active zone containing multiple stacked layers exhibit lasing wavelength at 1.55 ,m. On these devices, the experimental threshold current density reaches its minimum value for a double stacked QDH/QD structure. Other basic laser properties like gain and quantum efficiency are compared. QD lasers exhibit better threshold current densities but equivalent modal gain per layer than QDH. Finally, the analysis of the modal gain on QD laser structures shows a promising potential for improvement of the laser properties. (© 2009 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim) [source] Precursor complex structure of pseudouridine synthase TruB suggests coupling of active site perturbations to an RNA-sequestering peripheral protein domainPROTEIN SCIENCE, Issue 8 2005Charmaine Hoang Abstract The pseudouridine synthase TruB is responsible for the universally conserved post-transcriptional modification of residue 55 of elongator tRNAs. In addition to the active site, the "thumb," a peripheral domain unique to the TruB family of enzymes, makes extensive interactions with the substrate. To coordinate RNA binding and release with catalysis, the thumb may be able to sense progress of the reaction in the active site. To establish whether there is a structural correlate of communication between the active site and the RNA-sequestering thumb, we have solved the structure of a catalytically inactive point mutant of TruB in complex with a substrate RNA, and compared it to the previously determined structure of an active TruB bound to a reaction product. Superposition of the two structures shows that they are extremely similar, except in the active site and, intriguingly, in the relative position of the thumb. Because the two structures were solved using isomorphous crystals, and because the thumb is very well ordered in both structures, the displacement of the thumb we observe likely reflects preferential propagation of active site perturbations to this RNA-binding domain. One of the interactions between the active site and the thumb involves an active site residue whose hydrogen-bonding status changes during the reaction. This may allow the peripheral RNA-binding domain to monitor progress of the pseudouridylation reaction. [source] X-ray structure determination of the monoclinic (121,K) and orthorhombic (85,K) phases of langbeinite-type dithallium dicadmium sulfateACTA CRYSTALLOGRAPHICA SECTION B, Issue 6 2000A. Guelylah The structures of the monoclinic and the orthorhombic phases of type I langbeinite Tl2Cd2(SO4)3 have been determined at 121 and 85,K, respectively, by X-ray diffraction. A precise analysis of these structures shows the existence of some differences compared to langbeinites of type II. The monoclinic structure differs very little from the high-temperature cubic structure and the distortion relating the monoclinic structure to the cubic one is very small. SO4 tetrahedra seem to rotate under orthorhombic symmetry in the monoclinic phase. A symmetry distortion analysis of the ferroelectric monoclinic distortion discloses the importance of the secondary modes with orthorhombic symmetry, especially for the O atoms of the SO4 groups. [source] Structures of human MST3 kinase in complex with adenine, ADP and Mn2+ACTA CRYSTALLOGRAPHICA SECTION D, Issue 2 2010Tzu-Ping Ko The MST family is a subclass of mammalian serine/threonine kinases that are related to the yeast sterile-20 protein and are implicated in regulating cell growth and transformation. The MST3 protein contains a 300-residue catalytic domain and a 130-residue regulatory domain, which can be cleaved by caspase and activated by autophosphorylation, promoting apoptosis. Here, five crystal structures of the catalytic domain of MST3 are presented, including a complex with ADP and manganese, a unique cofactor preferred by the enzyme, and a complex with adenine. Similar to other protein kinases, the catalytic domain of MST3 folds into two lobes: the smaller N lobe forms the nucleotide-binding site and the larger C lobe recognizes the polypeptide substrate. The bound ADP and Mn2+ ions are covered by a glycine-rich loop and held in place by Asn149 and Asp162. A different orientation was observed for the ligand in the MST3,adenine complex. In the activation loop, the side chain of Thr178 is phosphorylated and is sandwiched by Arg143 and Arg176. Comparison of this structure with other similar kinase structures shows a 180° rotation of the loop, leading to activation of the enzyme. The well defined protein,ligand interactions also provide useful information for the design of potent inhibitors. [source] Structure of the restriction,modification controller protein C.Esp1396IACTA CRYSTALLOGRAPHICA SECTION D, Issue 9 2009N. Ball The controller protein of the Esp1396I restriction,modification (R,M) system binds differentially to three distinct operator sequences upstream of the methyltransferase (M) and endonuclease (R) genes to regulate the timing of gene expression. The crystal structure of a complex of the protein with two adjacent operator DNA sequences has been reported; however, the structure of the free protein has not yet been determined. Here, the crystal structure of the free protein is reported, with seven dimers in the asymmetric unit. Two of the 14 monomers show an alternative conformation to the major conformer in which the side chains of residues 43,46 in the loop region flanking the DNA-recognition helix are displaced by up to 10,Å. It is proposed that the adoption of these two conformational states may play a role in DNA-sequence promiscuity. The two alternative conformations are also found in the R35A mutant structure, which is otherwise identical to the native protein. Comparison of the free and bound protein structures shows a 1.4,Å displacement of the recognition helices when the dimer is bound to its DNA target. [source] Structure and sugar-specificity of basic winged-bean lectin: structures of new disaccharide complexes and a comparative study with other known disaccharide complexes of the lectinACTA CRYSTALLOGRAPHICA SECTION D, Issue 7 2008Kiran A. Kulkarni Crystal structures of the complexes of basic winged-bean agglutinin with the disaccharides Gal,1-4Gal (galabiose), Gal,1-6Glc (mellibiose) and Gal,1-4Gal,-Et have been determined and the complex with Gal,1-2Gal has been modelled. The interactions of the nonreducing Gal with the lectin at the primary site are the same as those in the known complexes with disaccharides having the ,1,3 linkage. The second residue in Gal,1-4Gal and Gal,1-6Glc forms a water bridge to the lectin, while the ethyl group in Gal,1-4Gal,-Et makes nonpolar interactions. In complexes involving disaccharides with ,1-3 linkages, which form part of the A and B blood-group substances, the second sugar residue forms a direct hydrogen bond to the variable loop in the binding site of the lectin. This in part explains the specificity of the lectin for the blood-group substances and also the higher affinity of ,1,3-linked disaccharides for the lectin compared with disaccharides involving other linkages. Including those reported here, 14 crystal structures involving the lectin, accounting for 54 crystallographically independent subunits, are available. A comparative study of these structures shows that the region involving the curved ,-sheet which nestles the metal ions is relatively rigid. The carbohydrate-binding region is perched on this region. The flat ,-sheet, which is involved in oligomerization and exhibits considerable variability in legume lectins, is relatively flexible. Indeed, the structures of basic winged-bean lectin have been of critical importance in establishing legume lectins as a family of proteins in which small alterations in essentially the same tertiary structure lead to large variations in quaternary association. They have also provided a structural explanation of the blood-group specificity of the lectin. [source] | |||||||||||||||||||||||||