High-resolution protein hydration NMR experiments: probing how protein surfaces interact with water and other non-covalent ligands |
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Authors: | Huang Hao Melacini Giuseppe |
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Affiliation: | Departments of Chemistry, Biochemistry and Biomedical Sciences, McMaster University, 1280 Main Street, W. Hamilton, Ont., Canada L8S 4M1 |
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Abstract: | High-resolution solution NMR experiments are extremely useful to characterize the location and the dynamics of hydrating water molecules at atomic resolution. However, these methods are severely limited by undesired incoherent transfer pathways such as those arising from exchange-relayed intra-molecular cross-relaxation. Here, we review several complementary exchange network editing methods that can be used in conjunction with other types of NMR hydration experiments such as magnetic relaxation dispersion and 1JNC′ measurements to circumvent these limitations. We also review several recent contributions illustrating how the original solution hydration NMR pulse sequence architecture has inspired new approaches to map other types of non-covalent interactions going well beyond the initial scope of hydration. Specifically, we will show how hydration NMR methods have evolved and have been adapted to binding site mapping, ligand screening, protein-peptide and peptide-lipid interaction profiling. |
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Keywords: | CT, constant time CTJ, CT quadrature-free J-resolved dimension DHPC, dihexanoyl phosphatylcholine DMF, N,N-dimethylformamide DMPC, dimyristoil phosphatylcholine DMSO, dymethyl-sulfoxide HIV, human immunodeficiency virus IR, infra red MD, molecular dynamics HMQC, hetero-nuclear multiple quantum coherence spectrum HSQC, hetero-nuclear single quantum coherence spectrum MRD, magnetic relaxation dispersion MS, mass spectrometry NMR, nuclear magnetic resonance NOE, nuclear overhauser effect NOESY, 2D-NOE spectroscopy PDB, protein data bank PFG, pulsed field gradient QF, quadrature-free ROE, rotating frame overhauser effect ROESY, 2D-ROE spectroscopy TROSY, transverse relaxation optimized spectroscopy XH, proton exchangeable with water |
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