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To fully understand biological function at an atomistic level, it is highly desirable to have knowledge of the structure and dynamics of biomolecules within living cells. High-resolution NMR spectroscopy is the only approach that can resolve 3D structures and dynamics of biomolecules in their native environment and has been shown to be efficiently applied to proteins in living cells. Here we show that paramagnetic NMR reduces the acquisition time of structural restraints in cells and together with GPS-Rosetta calculations is a remarkably efficient method to study proteins in cells.

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