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• W1521399553 abstract "The past year has seen important developments in NMR analysis of ligand binding. Several papers have illustrated the power of stable-isotope labeling and isotope-edited NMR in the investigation of large protein systems. Newly introduced techniques have been used to elucidate positions of bound water molecules, to define metal-ion-induced conformation changes, and to examine interactions involving paramagnetic ligands." @default.
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• W1521399553 date "1992-02-01" @default.
• W1521399553 modified "2023-09-25" @default.
• W1521399553 title "NMR analysis of ligand binding" @default.
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• W1521399553 doi "https://doi.org/10.1016/0959-440x(92)90176-8" @default.
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