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Solution‐State NMR Spectroscopy of a Seven‐Helix Transmembrane Protein Receptor: Backbone Assignment, Secondary Structure, and Dynamics
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Citations
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2008
Year
Proteinlipid InteractionProtein AssemblyBiomolecular Structure PredictionSecondary StructureMolecular BiologyAnalytical UltracentrifugationSequential Backbone AssignmentMacromolecular AssembliesBiophysicsBiochemistrySolution‐state Nmr SpectroscopyProtein Structure PredictionSolution Nmr SpectroscopyBiomolecular ScienceStructural BiologyDetergent SolutionBackbone DynamicsNatural SciencesProtein NmrMolecular BiophysicsMedicine
Protein in motion: A solution-state NMR study on the seven-helix transmembrane protein pSRII (see picture) in a detergent solution focused on the sequential backbone assignment, the characterization of the secondary structure, and the backbone dynamics. The structural integrity of the protein was confirmed, and mobility in the loops (ps–ns timescale) and slower motions in the helical core (μs–ms timescale) were identified. Supporting information for this article is available on the WWW under http://www.wiley-vch.de/contents/jc_2002/2008/z802783_s.pdf or from the author. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.
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