Haematology in mice after weekly blood sampling for 7 weeks

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Haematologic and Clinical Chemical values in 3 and 6 months old Göttingen minipigs

Blood samples were collected from sixty healthy Göttingen minipigs. fifteen males and fifteen females at the age of three months and fifteen males and fifteen females at the age of six months. The samples were taken at the breeder’s facilities. The samples were analysed for nineteen haematological and twenty~six clinical chemical parameters. Means, standard deviations and lowest and highest values are presented. In general the parameters were comparable with those reponed for other breeds of miniature and domestic swine. The white blood cell count, the percentages of neutrophils and monocytes and serum globulin levels were lower in these microbiologically defined minipigs compared with conventionally rearedpigs and minipigs. Three litter mates had a complex of abnormally high serum creatine kinase, lactate dehydrogenase, uspartate aminotransterase and alanine aminotmnsferase levels

Self-Assembly of Diamondoid Molecules and Derivatives (MD Simulations and DFT Calculations)

We report self-assembly and phase transition behavior of lower diamondoid molecules and their primary derivatives using molecular dynamics (MD) simulation and density functional theory (DFT) calculations. Two lower diamondoids (adamantane and diamantane), three adamantane derivatives (amantadine, memantine and rimantadine) and two artificial molecules (ADM•Na and DIM•Na) are studied separately in 125-molecule simulation systems. We performed DFT calculations to optimize their molecular geometries and obtained atomic electronic charges for the corresponding MD simulation, by which we predicted self-assembly structures and simulation trajectories for the seven different diamondoids and derivatives. Our radial distribution function and structure factor studies showed clear phase transitions and self-assemblies for the seven diamondoids and derivatives

S-33 constraints on the seawater sulfate contribution in modern seafloor hydrothermal vent sulfides

Author Posting. © Elsevier B.V., 2006. This is the author's version of the work. It is posted here by permission of Elsevier B.V. for personal use, not for redistribution. The definitive version was published in Geochimica et Cosmochimica Acta 71 (2007): 1170-1182, doi:10.1016/j.gca.2006.11.017.Sulfide sulfur in mid-oceanic ridge hydrothermal vents is derived from leaching of basaltic-sulfide and seawater-derived sulfate that is reduced during high temperature water rock interaction. Conventional sulfur isotope studies, however, are inconclusive about the mass-balance between the two sources because 34S/32S ratios of vent fluid H2S and chimney sulfide minerals may reflect not only the mixing ratio but also isotope exchange between sulfate and sulfide. Here, we show that high-precision analysis of S-33 can provide a unique constraint because isotope mixing and isotope exchange result in different Δ33S (≡ δ33S – 0.515 δ34S) values of up to 0.04 ‰ even if δ34S values are identical. Detection of such small Δ33S differences is technically feasible by using the SF6 dual-inlet mass-spectrometry protocol that has been improved to achieve a precision as good as 0.006 ‰ (2σ). Sulfide minerals (marcasite, pyrite, chalcopyrite, and sphalerite) and vent H2S collected from four active seafloor hydrothermal vent sites, East Pacific Rise (EPR) 9-10° N, 13° N, and 21° S and Mid-Atlantic Ridge (MAR) 37° N yield Δ33S values ranging from –0.002 to 0.033 and δ34S from –0.5 to 5.3 ‰. The combined δ34S and Δ33S systematics reveal that 73 to 89 % of vent sulfides are derived from leaching from basaltic sulfide and only 11 to 27 % from seawater-derived sulfate. Pyrite from EPR 13° N and marcasite from MAR 37° N are in isotope disequilibrium not only in δ34S but also in Δ33S with respect to associated sphalerite and chalcopyrite, suggesting non-equilibrium sulfur isotope exchange between seawater sulfate and sulfide during pyrite precipitation. Seafloor hydrothermal vent sulfides are characterized by low Δ33S values compared with biogenic sulfides, suggesting little or no contribution of sulfide from microbial sulfate reduction into hydrothermal sulfides at sediment-free mid-oceanic ridge systems. We conclude that 33S is an effective new tracer for interplay among seawater, oceanic crust and microbes in subseafloor hydrothermal sulfur cycles.S. Ono thanks the Agouron Institute for financial support and funding from the NASA Astrobiology Institute and Carnegie Institution of Washington for supporting the analytical costs. Funding for O. Rouxel is from the Deep Ocean Exploration Institute at WHOI

Exploring the conformational dynamics of alanine dipeptide in solution subjected to an external electric field: A nonequilibrium molecular dynamics simulation

In this paper, we investigate the conformational dynamics of alanine dipeptide under an external electric field by nonequilibrium molecular dynamics simulation. We consider the case of a constant and of an oscillatory field. In this context we propose a procedure to implement the temperature control, which removes the irrelevant thermal effects of the field. For the constant field different time-scales are identified in the conformational, dipole moment, and orientational dynamics. Moreover, we prove that the solvent structure only marginally changes when the external field is switched on. In the case of oscillatory field, the conformational changes are shown to be as strong as in the previous case, and non-trivial nonequilibrium circular paths in the conformation space are revealed by calculating the integrated net probability fluxes.Comment: 23 pages, 12 figure

Stability mechanisms of a thermophilic laccase probed by molecular dynamics.

Laccases are highly stable, industrially important enzymes capable of oxidizing a large range of substrates. Causes for their stability are, as for other proteins, poorly understood. In this work, multiple-seed molecular dynamics (MD) was applied to a Trametes versicolor laccase in response to variable ionic strengths, temperatures, and glycosylation status. Near-physiological conditions provided excellent agreement with the crystal structure (average RMSD ∼0.92 Å) and residual agreement with experimental B-factors. The persistence of backbone hydrogen bonds was identified as a key descriptor of structural response to environment, whereas solvent-accessibility, radius of gyration, and fluctuations were only locally relevant. Backbone hydrogen bonds decreased systematically with temperature in all simulations (∼9 per 50 K), probing structural changes associated with enthalpy-entropy compensation. Approaching T opt (∼350 K) from 300 K, this change correlated with a beginning "unzipping" of critical β-sheets. 0 M ionic strength triggered partial denucleation of the C-terminal (known experimentally to be sensitive) at 400 K, suggesting a general salt stabilization effect. In contrast, F(-) (but not Cl(-)) specifically impaired secondary structure by formation of strong hydrogen bonds with backbone NH, providing a mechanism for experimentally observed small anion destabilization, potentially remedied by site-directed mutagenesis at critical intrusion sites. N-glycosylation was found to support structural integrity by increasing persistent backbone hydrogen bonds by ∼4 across simulations, mainly via prevention of F(-) intrusion. Hydrogen-bond loss in distinct loop regions and ends of critical β-sheets suggest potential strategies for laboratory optimization of these industrially important enzymes

Factors That Drive Peptide Assembly and Fibril Formation: Experimental and Theoretical Analysis of Sup35 NNQQNY Mutants

Residue mutations have substantial effects on aggregation kinetics and propensities of amyloid peptides and their aggregate morphologies. Such effects are attributed to conformational transitions accessed by various types of oligomers such as steric zipper or single β-sheet. We have studied the aggregation propensities of six NNQQNY mutants: NVVVVY, NNVVNV, NNVVNY, VIQVVY, NVVQIY, and NVQVVY in water using a combination of ion-mobility mass spectrometry, transmission electron microscopy, atomic force microscopy, and all-atom molecular dynamics simulations. Our data show a strong correlation between the tendency to form early β-sheet oligomers and the subsequent aggregation propensity. Our molecular dynamics simulations indicate that the stability of a steric zipper structure can enhance the propensity for fibril formation. Such stability can be attained by either hydrophobic interactions in the mutant peptide or polar side-chain interdigitations in the wild-type peptide. The overall results display only modest agreement with the aggregation propensity prediction methods such as PASTA, Zyggregator, and RosettaProfile, suggesting the need for better parametrization and model peptides for these algorithms