Neill Richard Taylor

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The enzyme mechanism of sialidase from influenza virus has been investigated by kinetic isotope methods, NMR, and a molecular dynamics simulation of the enzyme-substrate complex. Comparison of the reaction rates obtained with the synthetic substrate 4-methylumbelliferyl-N-acetyl-alpha-D-neuraminic acid and the [3,3-2H]-substituted substrate revealed(More)
A molecular modeling study has been used to investigate the structural and energetic aspects of substrate and inhibitor binding and the mechanism of catalysis of influenza virus sialidase. A detailed analysis of the interactions of both N-acetylneuraminic acid (Neu5Ac,1) and a number of transition-state analogues with the active site of influenza A(More)
A two-beam differential laser absorption technique is used to measure 238U absorption spectra with high signal-to-noise ratios in an atmospheric pressure laser-induced plasma. High-resolution absorption spectra are presented for the 238U 861 nm transition in the presence of dry air at pressures up to 760 Torr. A spectral linewidth (FWHM) of 2.23±0.13 GHz(More)
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