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• W2336148972 abstract "This chapter presents a number of different methods for obtaining structural information on protein-bound ligands using NMR spectroscopy. For ligands that are in fast exchange between free and bound states, the transferred NOE can be used to obtain information on the bound conformation of the ligand and in some cases for delineating points of contact between the protein and the ligand. For tightly bound ligands, the techniques presented rely on the use of either isotopically labeled ligands or isotopically labeled protein to simplify the crowded spectra typically obtained for protein-ligand complexes. Isotope-selected experiments are useful for obtaining information on isotopically labeled ligands bound to unlabeled protein, whereas isotope-filtered experiments are useful for obtaining information on unlabeled ligands bound to isotopically labeled protein. Both methods are very robust and can provide information not only on the conformation of the bound ligand but also on portions of the ligand in close proximity to the protein. Three-dimensional heteronuclear NMR is an extension of isotope selected spectroscopy in which the heteronuclear frequencies of a labeled ligand are used to spread the proton resonances into a third dimension, providing even greater spectral simplification. In addition to these methods, techniques have been developed to elucidate the solvent-exposed regions of the bound ligand using a paramagnetic probe." @default.
• W2336148972 created "2016-06-24" @default.
• W2336148972 creator A5007570322 @default.
• W2336148972 creator A5076158972 @default.
• W2336148972 date "1994-01-01" @default.
• W2336148972 modified "2023-10-18" @default.
• W2336148972 title "[25] Nuclear magnetic resonance methods for studying protein-ligand complexes" @default.
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• W2336148972 doi "https://doi.org/10.1016/s0076-6879(94)39027-4" @default.
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