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NMR work in the solution state on proteins and nucleic acids, published in 2019, is reviewed. The chapter first covers methodological trends, in spectroscopy and areas such as isotopic labelling strategies, and reviews both commonly used approaches and less widely used methods. I review methodological developments in areas including accelerating acquisition, relaxation measurements and residual dipolar couplings and a miscellany of other advances. I then focus on two areas of particular interest: in-cell NMR and the study of intrinsically disordered proteins.

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