16,341 research outputs found

    Emulation of multivariate simulators using thin-plate splines with application to atmospheric dispersion

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    It is often desirable to build a statistical emulator of a complex computer simulator in order to perform analysis which would otherwise be computationally infeasible. We propose methodology to model multivariate output from a computer simulator taking into account output structure in the responses. The utility of this approach is demonstrated by applying it to a chemical and biological hazard prediction model. Predicting the hazard area which results from an accidental or deliberate chemical or biological release is imperative in civil and military planning and also in emergency response. The hazard area resulting from such a release is highly structured in space and we therefore propose the use of a thin-plate spline to capture the spatial structure and fit a Gaussian process emulator to the coefficients of the resultant basis functions. We compare and contrast four different techniques for emulating multivariate output: dimension-reduction using (i) a fully Bayesian approach with a principal component basis, (ii) a fully Bayesian approach with a thin-plate spline basis, assuming that the basis coefficients are independent, and (iii) a “plug-in” Bayesian approach with a thin-plate spline basis and a separable covariance structure; and (iv) a functional data modeling approach using a tensor-product (separable) Gaussian process. We develop methodology for the two thin-plate spline emulators and demonstrate that these emulators significantly outperform the principal component emulator. Further, the separable thin-plate spline emulator, which accounts for the dependence between basis coefficients, provides substantially more realistic quantification of uncertainty, and is also computationally more tractable, allowing fast emulation. For high resolution output data, it also offers substantial predictive and computational ad- vantages over the tensor-product Gaussian process emulator

    Frog foams and natural protein surfactants

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    Foams and surfactants are relatively rare in biology because of their potential to harm cell membranes and other delicate tissues. However, in recent work we have identified and characterized a number of natural surfactant proteins found in the foam nests of tropical frogs and other unusual sources. These proteins, and their associated foams, are relatively stable and bio-compatible, but with intriguing molecular structures that reveal a new class of surfactant activity. Here we review the structures and functional mechanisms of some of these proteins as revealed by experiments involving a range of biophysical and biochemical techniques, with additional mechanistic support coming from more recent site-directed mutagenesis studies

    Aqueous solubilization of C60 fullerene by natural protein surfactants, latherin and ranaspumin-2

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    C60 fullerene is not soluble in water and dispersion usually requires organic solvents, sonication or vigorous mechanical mixing. However, we show here that mixing of pristine C60 in water with natural surfactant proteins latherin and ranaspumin-2 (Rsn-2) at low concentrations yields stable aqueous dispersions with spectroscopic properties similar to those previously obtained by more vigorous methods. Particle sizes are significantly smaller than those achieved by mechanical dispersion alone, and concentrations are compatible with clusters approximating 1:1 protein:C60 stoichiometry. These proteins can also be adsorbed onto more intractable carbon nanotubes. This promises to be a convenient way to interface a range of hydrophobic nanoparticles and related materials with biological macromolecules, with potential to exploit the versatility of recombinant protein engineering in the development of nano-bio interface devices. It also has potential consequences for toxicological aspects of these and similar nanoparticles

    Resonance assignments for latherin, a natural surfactant protein from horse sweat

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    Latherin is an intrinsically surfactant protein of ~23 kDa found in the sweat and saliva of horses. Its function is probably to enhance the translocation of sweat water from the skin to the surface of the pelt for evaporative cooling. Its role in saliva may be to enhance the wetting, softening and maceration of the dry, fibrous food for which equines are adapted. Latherin is unusual in its relatively high content of aliphatic amino acids (~25 % leucines) that might contribute to its surfactant properties. Latherin is related to the palate, lung, and nasal epithelium carcinoma-associated proteins (PLUNCs) of mammals, at least one of which is now known to exhibit similar surfactant activity to latherin. No structures of any PLUNC protein are currently available. 15N,13C-labelled recombinant latherin was produced in Escherichia coli, and essentially all of the resonances were assigned despite the signal overlap due to the preponderance of leucines. The most notable exceptions include a number of residues located in an apparently dynamic loop region between residues 145 and 154. The assignments have been deposited with BMRB accession number 19067

    Experiment in beef production.

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    This bulletin gives the result of a year’s feeding test with steers of beef and dairy type; it also includes the slaughter test on the same animals, conducted in January, 1904, and a meat demonstration by Mr. John Gosling. While the results of the slaughter test are properly a part of the experiment, it has been deemed advisable to treat them somewhat distinctly. The data bearing on the differences in feeding and gaining capacity are therefore treated in the first part of the bulletin, and the results of the slaughter test, with Mr. Gosling’s explanations, in the latter part

    The feeding value of soft corn for beef production.

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    The early fall frosts affect the corn crop in the central and northern states more or less each year. The crop of 1902 was seriously damaged in many sections by the early September frost. The yield per acre was very much reduced. The percentage of marketable corn was a variable quantity. In some sections practically all of the corn was worthless from a regular market standpoint, due to the fact that it was too soft and watery for shipping purposes. This presented a serious condition of affairs. There was then but one way to utilize that portion of the crop which was soft and immature. It must be fed to live stock

    The structure of latherin, a surfactant allergen protein from horse sweat and saliva

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    Latherin is a highly surface-active allergen protein found in the sweat and saliva of horses and other equids. Its surfactant activity is intrinsic to the protein in its native form, and is manifest without associated lipids or glycosylation. Latherin probably functions as a wetting agent in evaporative cooling in horses, but it may also assist in mastication of fibrous food as well as inhibition of microbial biofilms. It is a member of the PLUNC family of proteins abundant in the oral cavity and saliva of mammals, one of which has also been shown to be a surfactant and capable of disrupting microbial biofilms. How these proteins work as surfactants while remaining soluble and cell membrane-compatible is not known. Nor have their structures previously been reported. We have used protein nuclear magnetic resonance spectroscopy to determine the conformation and dynamics of latherin in aqueous solution. The protein is a monomer in solution with a slightly curved cylindrical structure exhibiting a ‘super-roll’ motif comprising a four-stranded anti-parallel β-sheet and two opposing α-helices which twist along the long axis of the cylinder. One end of the molecule has prominent, flexible loops that contain a number of apolar amino acid side chains. This, together with previous biophysical observations, leads us to a plausible mechanism for surfactant activity in which the molecule is first localized to the non-polar interface via these loops, and then unfolds and flattens to expose its hydrophobic interior to the air or non-polar surface. Intrinsically surface-active proteins are relatively rare in nature, and this is the first structure of such a protein from mammals to be reported. Both its conformation and proposed method of action are different from other, non-mammalian surfactant proteins investigated so far

    Differential Increase in Taurine Levels by Low-Dose Ethanol in the Dorsal and Ventral Striatum Revealed by Microdialysis With On-Line Capillary Electrophoresis

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    Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/66164/1/01.ALC.0000131979.78003.34.pd

    Exact diagonalization of the S=1/2 Heisenberg antiferromagnet on finite bcc lattices to estimate properties on the infinite lattice

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    Here we generate finite bipartite body-centred cubic lattices up to 32 vertices. We have studied the spin one half Heisenberg antiferromagnet by diagonalizing its Hamiltonian on each of the finite lattices and hence computing its ground state properties. By extrapolation of these data we obtain estimates of the T = 0 properties on the infinite bcc lattice. Our estimate of the T = 0 energy agrees to five parts in ten thousand with third order spin wave and series expansion method estimates, while our estimate of the staggered magnetization agrees with the spin wave estimate to within a quarter of one percent.Comment: 16 pages, LaTeX, 1 ps figure, to appear in J.Phys.
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