Spin labels

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  • After opening a new class of chemical reactions in 1964, reactions in which unpaired electrons of stable radicals were not involved, nitroxide (aminoxyl) radicals became one of the most interesting and rapidly developing area of modern physical chemistry with their application to biophysics, molecular biology, polymer sciences and medicine. Further development of this field depends on new pathways in the nitroxide chemistry, modern methods in EPR spectroscopy and revealing new perspective practical approaches....

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  • EPR spectroscopy, performed after site-directed spin-labeling, was used to study structural dynamics in a cold-adapted alkaline phosphatase (EC 3.1.1.1). Differences in the structural environment of six spin-labeled side chains allowed them to be classified (with reference to previously obtained mobility maps) as belonging to loop positions (either relatively surface exposed or in structural contact) or helix positions (surface exposed, in contact, or buried).

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  • Conventional and saturation transfer electron paramagnetic resonance spectroscopy (EPR and ST EPR) was used to study the orientation of probe molecules in muscle fibers in different intermediate states of the ATP hydrolysis cycle. A separate procedure was used to obtain ST EPR spectra with precise phase settings even in the case of samples with low spectral intensity. Fibers prepared from rabbit psoas muscle were labeled with isothiocyanate spin labels at the reactive thiol sites of the catalytic domain of myosin....

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  • bR, N-like and O-like intermediate states of [ 15 N]methionine-labelled wild type and D85N⁄T170C bacteriorhodopsin were accumulated in native membranes by controlling the pH of the preparations. 15 N cross polariza-tion and magic angle sample spinning (CPMAS) NMR spectroscopy allowed resolution of seven out of nine resonances in the bR-state. It was possible to assign some of the observed resonances by using 13 C⁄ 15 N rota

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