To what extent can mutual shifting of folded carbonaceous walls in slit-like pores affect their adsorption properties?

We have performed systematic Monte Carlo studies on the influence of shifting the walls in slit-like systems constructed from folded graphene sheets on their adsorption properties. Specifically, we have analysed the effect on the mechanism of argon adsorption (T = 87 K) and on adsorption and separation of three binary gas mixtures: CO2/N2, CO2/CH4 and CH4/N2 (T = 298 K). The effects of the changes in interlayer distance were also determined. We show that folding of the walls significantly improves the adsorption and separation properties in comparison to ideal slit-like systems. Moreover, we demonstrate that mutual shift of sheets (for small interlayer distances) causes the appearance of small pores between opposite bulges. This causes an increase in vapour adsorption at low pressures. Due to overlapping of interactions with opposite walls causing an increase in adsorption energy, the mutual shift of sheets is also connected with the rise in efficiency of mixtures separation. The effects connected with sheet orientation vanish as the interlayer distance increases.

In situ observations in cyclones over Fram Strait

During the international FRAMZY expedition in March 2002 in-situ observations of Fram Strait cyclones were made by aircraft, ship and automatic buoys in order to study the interaction between cyclones and sea ice. The atmospheric characteristics of the observed cyclones are presented in this paper. The cyclones were generated in the baroclinic zone at the ice edge and moved NNE-ward along the ice edge. This was supported by warm air advection from WSW by an upper-level wave. The cyclones were rather small (diameter 200– 700 km) and shallow (1–1.5 km e-folding height for the horizontal pressure and temperature difference) with life times between 12 and 36 hours. In spite of the small space and time scales, remarkable extremes were observed within the cyclones. Winds reached maxima above 20 ms−1 lasting for only a few hours. The transition from the cold to the advancing warm air over sea ice occurred within narrow (5–30 km) frontal zones in which vorticity and convergence reached maxima on the order of 10−3 s−1. It is discussed whether the sea ice in spite of its inertia is able to react on these strong sub cyclone-scale processes and, thus, these processes have to be taken into account in models in order to simulate the cyclone-sea ice interaction properly.

Intracellular trafficking, localization, and mobilization of platelet-borne thiol isomerases

OBJECTIVE: Thiol isomerases facilitate protein folding in the endoplasmic reticulum, and several of these enzymes, including protein disulfide isomerase and ERp57, are mobilized to the surface of activated platelets, where they influence platelet aggregation, blood coagulation, and thrombus formation. In this study, we examined the synthesis and trafficking of thiol isomerases in megakaryocytes, determined their subcellular localization in platelets, and identified the cellular events responsible for their movement to the platelet surface on activation. APPROACH AND RESULTS: Immunofluorescence microscopy imaging was used to localize protein disulfide isomerase and ERp57 in murine and human megakaryocytes at various developmental stages. Immunofluorescence microscopy and subcellular fractionation analysis were used to localize these proteins in platelets to a compartment distinct from known secretory vesicles that overlaps with an inner cell-surface membrane region defined by the endoplasmic/sarcoplasmic reticulum proteins calnexin and sarco/endoplasmic reticulum calcium ATPase 3. Immunofluorescence microscopy and flow cytometry were used to monitor thiol isomerase mobilization in activated platelets in the presence and absence of actin polymerization (inhibited by latrunculin) and in the presence or absence of membrane fusion mediated by Munc13-4 (absent in platelets from Unc13dJinx mice). CONCLUSIONS: Platelet-borne thiol isomerases are trafficked independently of secretory granule contents in megakaryocytes and become concentrated in a subcellular compartment near the inner surface of the platelet outer membrane corresponding to the sarco/endoplasmic reticulum of these cells. Thiol isomerases are mobilized to the surface of activated platelets via a process that requires actin polymerization but not soluble N-ethylmaleimide-sensitive fusion protein attachment receptor/Munc13-4-dependent vesicular-plasma membrane fusion.

Tissue distribution of quiescin Q6/sulfhydryl oxidase (QSOX) in developing mouse

Quiescin Q6/sulfhydryl oxidases (QSOX) are revisited thiol oxidases considered to be involved in the oxidative protein folding, cell cycle control and extracellular matrix remodeling. They contain thioredoxin domains and introduce disulfide bonds into proteins and peptides, with the concomitant hydrogen peroxide formation, likely altering the redox environment. Since it is known that several developmental processes are regulated by the redox state, here we assessed if QSOX could have a role during mouse fetal development. For this purpose, an anti-recombinant mouse QSOX antibody was produced and characterized. In E-13.5, E-16.5 fetal tissues, QSOX immunostaining was confined to mesoderm- and ectoderm-derived tissues, while in P1 neonatal tissues it was slightly extended to some endoderm-derived tissues. QSOX expression, particularly by epithelial tissues, seemed to be developmentally-regulated, increasing with tissue maturation. QSOX was observed in loose connective tissues in all stages analyzed, intra and possibly extracellularly, in agreement with its putative role in oxidative folding and extracellular matrix remodeling. In conclusion, QSOX is expressed in several tissues during mouse development, but preferentially in those derived from mesoderm and ectoderm, suggesting it could be of relevance during developmental processes.

Biochemical characterization of serine acetyltransferase and cysteine desulfhydrase from Leishmania major

Cysteine metabolism exhibits atypical features in Leishmania parasites. The nucleotide sequence annotated as LmjF32.2640 encodes a cysteine desulfhydrase, which specifically catalyzes the breakdown of cysteine into pyruvate, NH(3) and H(2)S. Like in other pathogens, this capacity might be associated with regulatory mechanisms to control the intracellular level of cysteine, a highly toxic albeit essential amino acid, in addition to generate pyruvate for energy production. Besides, our results provide the first insight into the biochemical properties of Leishmania major serine acetyltransferase (SAT), which is likely involved in the two routes for de novo synthesis of cysteine in this pathogen. When compared with other members of SAT family, the N-terminal region of L. major homologue is uniquely extended, and seems to be essential for proper protein folding. Furthermore, unlike plant and bacterial enzymes, the carboxy-terminal-C(10) sequence stretch of L major SAT appears not to be implicated in forming a tight bi-enzyme complex with cysteine synthase. (C) 2010 Elsevier B.V. All rights reserved.

Probing the (6,7)Li nucleon densities through a new break-up process approach

In this work we present a double folding optical model analysis of new near-barrier quasi-elastic experimental data for the (6,7)Li + (120)Sn systems. From the analysis, it was possible to confirm the ground-state nucleon densities assumed for the weakly bound (6,7)Li isotopes. The apparent discrepancies between the experimental densities and those based on Dirac-Hartree-Fock Bogoliubov (DHB) calculations were removed. A new approach that simulates the projectile break-up and a positive polarization from couplings of (6,7)Li bound states with the continuum was considered in the reaction mechanism. (C) 2010 Elsevier B.V. All rights reserved.

Understanding fusion suppression and enhancement in the (18)O+(58,60,64)Ni systems

Realistic coupled-channel calculation results for the (18)[O] + (58,60,64)Ni systems in the bombarding energy range 34.5 <= E(Lab) <= 6-5 MeV are presented. The overall agreement with existing experimental data is quite good. Our calculations predict an unexpected fusion suppression for above-barrier energies, with an important contribution of the two neutron ((18)O, (16)O) transfer channel couplings. The sub-barrier fusion enhancement and the above barrier suppression, predicted by the calculations, are consistent with the nuclear structure of the Ni region. Comparisons with recently reported similar effects in reactions induced by the (6)He projectile are discussed. (C) 2009 Elsevier B.V. All rights reserved.

An imaginary potential with universal normalization for dissipative processes in heavy-ion reactions

In this work we present new coupled channel calculations with the Sao Paulo potential (SPP) as the bare interaction, and an imaginary potential with system and energy independent normalization that has been developed to take into account dissipative processes in heavy-ion reactions. This imaginary potential is based on high-energy nucleon interaction in nuclear medium. Our theoretical predictions for energies up to approximate to 100 MeV/nucleon agree very well with the experimental data for the p, n + nucleus, (16)O + (27)Al, (16)O + (60)Ni, (58)Ni + (124)Sn, and weakly bound projectile (7)Li + (120)Sn systems. (C) 2008 Elsevier B.V. All rights reserved.

Study of (9)Be+(12)C elastic scattering at energies near the Coulomb barrier

In this work, angular distribution measurements for the elastic channel were performed for the (9)Be + (12)C reaction at the energies E(Lab) = 13.0, 14.5, 17.3, 19.0 and 21.0 MeV, near the Coulomb barrier. The data have been analyzed in the framework of the double folding Sao Paulo potential. The experimental elastic scattering angular distributions were well described by the optical potential at forward angles for all measured energies. However, for the three highest energies, an enhancement was observed for intermediate and backward angles. This can be explained by the elastic transfer mechanism. (C) 2011 Elsevier B.V. All rights reserved.

Total reaction cross-sections for light weakly bound systems

We have measured the elastic scattering cross-section for (8)Li + (9)Be and (8)Li + (51)V systems at 19.6 MeV and 18.5 MeV, respectively. We have also extracted total reaction cross sections from the elastic scattering analysis for several light weakly bound systems using the optical model with Woods-Saxon and double-folding-type potentials. Different reduction methods for the total reaction cross-sections have been applied to analyze and compare simultaneously all the systems.

Temperature effects on a network of dissipative quantum harmonic oscillators: collective damping and dispersion processes

In this paper we extend the results presented in (de Ponte, Mizrahi and Moussa 2007 Phys. Rev. A 76 032101) to treat quantitatively the effects of reservoirs at finite temperature in a bosonic dissipative network: a chain of coupled harmonic oscillators whatever its topology, i.e., whichever the way the oscillators are coupled together, the strength of their couplings and their natural frequencies. Starting with the case where distinct reservoirs are considered, each one coupled to a corresponding oscillator, we also analyze the case where a common reservoir is assigned to the whole network. Master equations are derived for both situations and both regimes of weak and strong coupling strengths between the network oscillators. Solutions of these master equations are presented through the normal ordered characteristic function. These solutions are shown to be significantly involved when temperature effects are considered, making difficult the analysis of collective decoherence and dispersion in dissipative bosonic networks. To circumvent these difficulties, we turn to the Wigner distribution function which enables us to present a technique to estimate the decoherence time of network states. Our technique proceeds by computing separately the effects of dispersion and the attenuation of the interference terms of the Wigner function. A detailed analysis of the dispersion mechanism is also presented through the evolution of the Wigner function. The interesting collective dispersion effects are discussed and applied to the analysis of decoherence of a class of network states. Finally, the entropy and the entanglement of a pure bipartite system are discussed.

Thermodynamic characterization of the palm tree Roystonea regia peroxidase stability

The structural stability of a peroxidase, a dimeric protein from royal palm tree (Roystonea regia) leaves, has been characterized by high-sensitivity differential scanning calorimetry, circular dichroism, steady-state tryptophan fluorescence and analytical ultracentifugation under different solvent conditions. It is shown that the thermal and chemical (using guanidine hydrochloride (Gdn-HCl)) folding/unfolding of royal palm tree peroxidase (RPTP) at pH 7 is a reversible process involving a highly cooperative transition between the folded dimer and unfolded monomers, with a free stabilization energy of about 23 kcal per mol of monomer at 25 degrees C. The structural stability of RPTP is pH-dependent. At pH 3, where ion pairs have disappeared due to protonation, the thermally induced denaturation of RPTP is irreversible and strongly dependent upon the scan rate, suggesting that this process is under kinetic control. Moreover, thermally induced transitions at this pH value are dependent on the protein concentration, allowing it to be concluded that in solution RPTP behaves as dimer, which undergoes thermal denaturation coupled with dissociation. Analysis of the kinetic parameters of RPTP denaturation at pH 3 was accomplished on the basis of the simple kinetic scheme N ->(k) D, where k is a first-order kinetic constant that changes with temperature, as given by the Arrhenius equation; N is the native state, and D is the denatured state, and thermodynamic information was obtained by extrapolation of the kinetic transition parameters to an infinite heating rate. Obtained in this way, the value of RPTP stability at 25 degrees C is ca. 8 kcal per mole of monomer lower than at pH 7. In all probability, this quantity reflects the contribution of ion pair interactions to the structural stability of RPTP. From a comparison of the stability of RPTP with other plant peroxidases it is proposed that one of the main factors responsible for the unusually high stability of RPTP which enhances its potential use for biotechnological purposes, is its dimerization. (c) 2008 Elsevier Masson SAS. All rights reserved.

Structural modeling and mutational analysis of yeast eukaryotic translation initiation factor 5A reveal new critical residues and reinforce its involvement in protein synthesis

Eukaryotic translation initiation factor 5A (eIF5A) is a protein that is highly conserved and essential for cell viability. This factor is the only protein known to contain the unique and essential amino acid residue hypusine. This work focused on the structural and functional characterization of Saccharomyces cerevisiae eIF5A. The tertiary structure of yeast eIF5A was modeled based on the structure of its Leishmania mexicana homologue and this model was used to predict the structural localization of new site-directed and randomly generated mutations. Most of the 40 new mutants exhibited phenotypes that resulted from eIF-5A protein-folding defects. Our data provided evidence that the C-terminal alpha-helix present in yeast eIF5A is an essential structural element, whereas the eIF5A N-terminal 10 amino acid extension not present in archaeal eIF5A homologs, is not. Moreover, the mutants containing substitutions at or in the vicinity of the hypusine modification site displayed nonviable or temperature-sensitive phenotypes and were defective in hypusine modification. Interestingly, two of the temperature-sensitive strains produced stable mutant eIF5A proteins - eIF5A(K56A) and eIF5A(Q22H,L93F)- and showed defects in protein synthesis at the restrictive temperature. Our data revealed important structural features of eIF5A that are required for its vital role in cell viability and underscored an essential function of eIF5A in the translation step of gene expression.

Analysis of Agonist and Antagonist Effects on Thyroid Hormone Receptor Conformation by Hydrogen/Deuterium Exchange

Thyroid hormone receptors (TRs) are ligand-gated transcription factors with critical roles in development and metabolism. Although x-ray structures of TR ligand-binding domains (LBDs) with agonists are available, comparable structures without ligand (apo-TR) or with antagonists are not. It remains important to understand apo-LBD conformation and the way that it rearranges with ligands to develop better TR pharmaceuticals. In this study, we conducted hydrogen/deuterium exchange on TR LBDs with or without agonist (T(3)) or antagonist (NH(3)). Both ligands reduce deuterium incorporation into LBD amide hydrogens, implying tighter overall folding of the domain. As predicted, mass spectroscopic analysis of individual proteolytic peptides after hydrogen/deuterium exchange reveals that ligand increases the degree of solvent protection of regions close to the buried ligand-binding pocket. However, there is also extensive ligand protection of other regions, including the dimer surface at H10-H11, providing evidence for allosteric communication between the ligand-binding pocket and distant interaction surfaces. Surprisingly, C-terminal activation helix H12, which is known to alter position with ligand, remains relatively protected from solvent in all conditions suggesting that it is packed against the LBD irrespective of the presence or type of ligand. T(3), but not NH(3), increases accessibility of the upper part of H3-H5 to solvent, and we propose that TR H12 interacts with this region in apo-TR and that this interaction is blocked by T(3) but not NH(3.) We present data from site-directed mutagenesis experiments and molecular dynamics simulations that lend support to this structural model of apo-TR and its ligand-dependent conformational changes. (Molecular Endocrinology 25: 15-31, 2011)

Camptosemin, a tetrameric lectin of Camptosema ellipticum: structural and functional analysis

Lectins have been classified into a structurally diverse group of proteins that bind carbohydrates and glycoconjugates with high specificity. They are extremely useful molecules in the characterization of saccharides, as drug delivery mediators, and even as cellular surface makers. In this study, we present camptosemin, a new lectin from Camptosema ellipticum. It was characterized as an N-acetyl-d-galactosamine-binding homo-tetrameric lectin, with a molecular weight around 26 kDa/monomers. The monomers were stable over a wide range of pH values and exhibited pH-dependent oligomerization. Camptosemin promoted adhesion of breast cancer cells and hemagglutination, and both activities were inhibited by its binding of sugar. The stability and unfolding/folding behavior of this lectin was characterized using fluorescence and far-UV circular dichroism spectroscopies. The results indicate that chemical unfolding of camptosemin proceeds as a two-state monomer-tetramer process. In addition, small-angle X-ray scattering shows that camptosemin behaves as a soluble and stable homo-tetramer molecule in solution.