27 research outputs found

    Solution structure of the coxsackievirus and adenovirus receptor domain 1

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    The coxsackievirus and adenovirus receptor (CAR) mediates entry of coxsackievirus B (CVB) and adenovirus (Ad). The normal cellular function of CAR, which is expressed in a wide variety of tissue types, is thought to involve homophilic cell adhesion in the developing brain. The extracellular domain of CAR consists of two immunoglobulin (Ig) domains termed CAR-D1 and CAR-D2. CAR-D1 is shown by sedimentation velocity to be monomeric at pH 3.0. The solution structure and the dynamic properties of monomeric CAR-D1 have been determined by NMR spectroscopy at pH 3.0. The determinants of the CAR-D1 monomer−dimer equilibrium, as well as the binding site of CVB and Ad on CAR, are discussed in light of the monomer structure

    Nonequilibrium dissipation scaling in large Reynolds number turbulence generated by rectangular fractal grids

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    In this paper, the turbulence fields generated by a group of modified fractal grids, referred to as the rectangular fractal grids (RFGs), are documented and discussed. The experiments were carried out using hot-wire anemometry in three facilities at Imperial College London and the Laboratory of Fluid Mechanics in Lille, France. Due to the large Reynolds number of the resulting turbulence, several data processing methods for turbulence properties are carefully evaluated. Two spectral models were adopted, respectively, to correct the large and small wave-number ranges of the measured spectrum. After the technical discussion, the measurement results are presented in terms of one-point statistics, length scales, homogeneity, isotropy, and dissipation. The main conclusions are twofold. First, the location of maximum turbulence intensity x_peak is shown to be independent of the inlet Reynolds number but dependent on the ratio between the lengths of the largest grid bars in the transverse and vertical directions. This is crucial to the production of prescribed features of turbulent flows in laboratory. Second, these RFG-generated turbulent flows are shown to be quasi-homogeneous in the decay region for x/x_peak>1.5, but the isotropy is poorer than that of the previous studied fractal square grid-generated turbulence. In the beginning of the decay region, a decreasing pattern of the integral length scale L_u and Taylor microscale λ was observed, yet the ratio L_u/λ remained roughly constant along the centerline, so C_ε∼Re^(−1) λ, complying with the nonequilibrium scaling relation reported in previous studies for various turbulent flows

    Solution Structure of the Coxsackievirus and Adenovirus Receptor Domain 1<sup>†</sup><sup>,</sup><sup>‡</sup>

    No full text
    The coxsackievirus and adenovirus receptor (CAR) mediates entry of coxsackievirus B (CVB) and adenovirus (Ad). The normal cellular function of CAR, which is expressed in a wide variety of tissue types, is thought to involve homophilic cell adhesion in the developing brain. The extracellular domain of CAR consists of two immunoglobulin (Ig) domains termed CAR-D1 and CAR-D2. CAR-D1 is shown by sedimentation velocity to be monomeric at pH 3.0. The solution structure and the dynamic properties of monomeric CAR-D1 have been determined by NMR spectroscopy at pH 3.0. The determinants of the CAR-D1 monomer−dimer equilibrium, as well as the binding site of CVB and Ad on CAR, are discussed in light of the monomer structure
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