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- W78543485 abstract "Electron paramagnetic resonance (EPR) spectroscopy of site-directed spin labelled biomolecules (site-directed spin labelling, SDSL) has emerged as a powerful method for studying the structure and conformational dynamics of proteins and nucleic acids under conditions relevant to function. In this technique, a spin label side chain is introduced at a selected site via cysteine substitution mutagenesis followed by modification of the unique sulfhydryl group with a specific paramagnetic nitroxide reagent (Fig. 1). The continuous wave (cw) EPR spectrum yields information about the nitroxide side chain mobility, the solvent accessibility, the polarity of its immediate environment and the distance between the nitroxide and another paramagnetic centre in the protein. EPR data analysis of a series of spin labelled variants of a given protein allows definition of elements of secondary structure, including their solvent exposure, to characterize protein topography and to determine orientations of individual segments of the protein. A complete analysis allows modelling of protein structures with a spatial resolution at the level of the backbone fold 3, . The method is applicable to any protein that retains its function after spin labelling. One of the most powerful properties of the method is its sensitivity to molecular dynamics: protein equilibrium fluctuations and conformational" @default.
- W78543485 created "2016-06-24" @default.
- W78543485 creator A5031425189 @default.
- W78543485 date "2005-12-30" @default.
- W78543485 modified "2023-09-23" @default.
- W78543485 title "Multi-Frequency EPR Spectroscopy Studies of the Structure and Conformational Changes of Site-Directed Spin Labelled Membrane Proteins" @default.
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- W78543485 doi "https://doi.org/10.1007/0-306-48662-8_10" @default.
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