2,288 research outputs found

    Mean-field transfer-matrix study of the magnetic phase diagram of CsNiF3_{\bf 3}

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    A method for treating ferromagnetic chains coupled with antiferromagnetic interactions on an hexagonal lattice is presented in this paper. The solution of the 1D1D part of the problem is obtained by classical transfer-matrix while the coupling between the chains is processed by mean-field theory. This method is applied with success to the phase diagram and angular dependence of the critical field of CsNiF3_3. Results concerning the general influence of single-ion anisotropy on the magnetic ordering of such systems are also presented.Comment: J1K 2R1 14 pages (RevTex 3.0 preprint), 7 Postscript figures uuencoded at the end, Report# CRPS-94-2

    Engineered thermostable fungal cellulases exhibit efficient synergistic cellulose hydrolysis at elevated temperatures

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    A major obstacle to using widely available and low-cost lignocellulosic feedstocks to produce renewable fuels and chemicals is the high cost and low efficiency of the enzyme mixtures used to hydrolyze cellulose to fermentable sugars. One possible solution entails engineering current cellulases to function efficiently at elevated temperatures in order to boost reaction rates and exploit several other advantages of a higher temperature process. Here we describe the creation of the most stable reported fungal endoglucanase, a derivative of Hypocrea jecorina (anamorph Trichoderma reesei) Cel5A, by combining stabilizing mutations identified using consensus design, chimera studies, and structure-based computational methods. The engineered endoglucanase has an optimal temperature that is 17 °C higher than wild type H. jecorina Cel5A, and hydrolyzes 1.5 times as much cellulose over 60 h at its optimum temperature compared to the wild type enzyme at its optimal temperature.This enzyme complements previously-engineered highly-active, thermostable variants of the fungal cellobiohydrolases Cel6A and Cel7A in a thermostable cellulase mixture that hydrolyzes cellulose synergistically at an optimum temperature of 70 °C over 60 h.The thermostable mixture produces three times as much total sugar as the best mixture of the wild type enzymes operating at its optimum temperature of 60 °C, clearly demonstrating the advantage of higher-temperature cellulose hydrolysis

    Comparison of Family 9 Cellulases from Mesophilic and Thermophilic Bacteria

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    Cellulases containing a family 9 catalytic domain and a family 3c cellulose binding module (CBM3c) are important components of bacterial cellulolytic systems. We measured the temperature dependence of the activities of three homologs: Clostridium cellulolyticum Cel9G, Thermobifida fusca Cel9A, and C. thermocellum Cel9I. To directly compare their catalytic activities, we constructed six new versions of the enzymes in which the three GH9-CBM3c domains were fused to a dockerin both with and without a T. fusca fibronectin type 3 homology module (Fn3). We studied the activities of these enzymes on crystalline cellulose alone and in complex with a miniscaffoldin containing a cohesin and a CBM3a. The presence of Fn3 had no measurable effect on thermostability or cellulase activity. The GH9-CBM3c domains of Cel9A and Cel9I, however, were more active than the wild type when fused to a dockerin complexed to scaffoldin. The three cellulases in complex have similar activities on crystalline cellulose up to 60°C, but C. thermocellum Cel9I, the most thermostable of the three, remains highly active up to 80°C, where its activity is 1.9 times higher than at 60°C. We also compared the temperature-dependent activities of different versions of Cel9I (wild type or in complex with a miniscaffoldin) and found that the thermostable CBM is necessary for activity on crystalline cellulose at high temperatures. These results illustrate the significant benefits of working with thermostable enzymes at high temperatures, as well as the importance of retaining the stability of all modules involved in cellulose degradation

    A Data-Driven Design Evaluation Tool for Handheld Device Soft Keyboards

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    Thumb interaction is a primary technique used to operate small handheld devices such as smartphones. Despite the different techniques involved in operating a handheld device compared to a personal computer, the keyboard layouts for both devices are similar. A handheld device keyboard that considers the physical capabilities of the thumb may improve user experience. We developed and applied a design evaluation tool for different geometries of the QWERTY keyboard using a performance evaluation model. The model utilizes previously collected data on thumb motor performance and posture for different tap locations and thumb movement directions. We calculated a performance index (PITOT, 0 is worst and 2 is best) for 663 designs consisting in different combinations of three variables: the keyboard's radius of curvature (R) (mm), orientation (O) (°), and vertical location on the screen (L). The current standard keyboard performed poorly (PITOT = 0.28) compared to other designs considered. Keyboard location (L) contributed to the greatest variability in performance out of the three design variables, suggesting that designers should modify this variable first. Performance was greatest for designs in the middle keyboard location. In addition, having a slightly upward curve (R = −20 mm) and orientated perpendicular to the thumb's long axis (O = −20°) improved performance to PITOT = 1.97. Poorest performances were associated with placement of the keyboard's spacebar in the bottom right corner of the screen (e.g., the worst was for R = 20 mm, O = 40°, L = Bottom (PITOT = 0.09)). While this evaluation tool can be used in the design process as an ergonomic reference to promote user motor performance, other design variables such as visual access and usability still remain unexplored

    JRNL 370.01: Beat Reporting

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    Tyrosine Flourescence to Monitor the Denaturation of a Bacterial Protein

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    Tyrosine fluorescence was used to monitor the denaturation of a protein. The protein used as our model system was the regulatory subunit (RSU) of aspartate transcarbamoylase from E. coli. RSU is a dimer of two identical chains with one zinc ion bound per chain. It is also a typtophan-deficient protein so tyrosine flourescence was used as a probe to monitor changes during denaturation

    JRNL 301X.01: Diversity in Media

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    Fourier and Gegenbauer expansions for a fundamental solution of the Laplacian in the hyperboloid model of hyperbolic geometry

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    Due to the isotropy dd-dimensional hyperbolic space, there exist a spherically symmetric fundamental solution for its corresponding Laplace-Beltrami operator. On the RR-radius hyperboloid model of dd-dimensional hyperbolic geometry with R>0R>0 and d2d\ge 2, we compute azimuthal Fourier expansions for a fundamental solution of Laplace's equation. For d2d\ge 2, we compute a Gegenbauer polynomial expansion in geodesic polar coordinates for a fundamental solution of Laplace's equation on this negative-constant sectional curvature Riemannian manifold. In three-dimensions, an addition theorem for the azimuthal Fourier coefficients of a fundamental solution for Laplace's equation is obtained through comparison with its corresponding Gegenbauer expansion.Comment: arXiv admin note: substantial text overlap with arXiv:1201.440
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