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- W2086133094 abstract "Historically, the task of determining the structure of membrane proteins has been hindered by experimental difficulties associated with their lipid-embedded domains. Here, we provide an overview of recently developed experimental and predictive tools that are changing our view of this largely unexplored territory - the 'Wild West' of structural biology. Crystallography, single-particle methods and atomic force microscopy are being used to study huge membrane proteins with increasing detail. Solid-state nuclear magnetic resonance strategies provide orientational constraints for structure determination of transmembrane (TM) alpha-helices and accurate measurements of intramolecular distances, even in very complex systems. Longer distance constraints are determined by site-directed spin-labelling electron paramagnetic resonance, but current labelling strategies still constitute some limitation. Other methods, such as site-specific infrared dichroism, enable orientational analysis of TM alpha-helices in aligned bilayers and, combined with novel computational and predictive tools that use evolutionary conservation data, are being used to analyze TM alpha-helical bundles." @default.
- W2086133094 created "2016-06-24" @default.
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- W2086133094 date "2003-03-01" @default.
- W2086133094 modified "2023-10-18" @default.
- W2086133094 title "Membrane proteins: the ‘Wild West’ of structural biology" @default.
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- W2086133094 doi "https://doi.org/10.1016/s0968-0004(03)00026-4" @default.
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