ArticleJournal of biomolecular NMR2006
Utilization of methyl proton resonances in cross-saturation measurement for determining the interfaces of large protein-protein complexes.
Article in Journal of biomolecular NMR, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Mapping Human Monoclonal IgE Epitopes on the Major Dust Mite Allergen Der p 2.Journal of immunology (Baltimore, Md. : 1950) · 2020Article
- Methyl-selective isotope labeling using α-ketoisovalerate for the yeast Pichia pastoris recombinant protein expression system.Journal of biomolecular NMR · 2018Article
- Current NMR Techniques for Structure-Based Drug Discovery.Molecules (Basel, Switzerland) · 2018Review
- An allosteric conduit facilitates dynamic multisite substrate recognition by the SCFNature communications · 2017Article
- Identification of Hydrophobic Interfaces in Protein-Ligand Complexes by Selective Saturation Transfer NMR Spectroscopy.Molecules (Basel, Switzerland) · 2015Article
- The solution structure, binding properties, and dynamics of the bacterial siderophore-binding protein FepB.The Journal of biological chemistry · 2014Article
- NMR disentangles a dynamic disaggregase machinery.Nature structural & molecular biology · 2013Article
- On the role of NMR spectroscopy for characterization of antimicrobial peptides.Methods in molecular biology (Clifton, N.J.) · 2013Review
- Structural basis for modulation of gating property of G protein-gated inwardly rectifying potassium ion channel (GIRK) by i/o-family G protein α subunit (Gαi/o).The Journal of biological chemistry · 2012Article
- Structural basis for the activation of platelet integrin αIIbβ3 by calcium- and integrin-binding protein 1.Journal of the American Chemical Society · 2012Article
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- Structural NMR of protein oligomers using hybrid methods.Journal of structural biology · 2011Review
- NMR analyses of the Gbetagamma binding and conformational rearrangements of the cytoplasmic pore of G protein-activated inwardly rectifying potassium channel 1 (GIRK1).The Journal of biological chemistry · 2011Article
- Structural determination of biomolecular interfaces by nuclear magnetic resonance of proteins with reduced proton density.Journal of biomolecular NMR · 2010Article
- Structural basis of the interaction between chemokine stromal cell-derived factor-1/CXCL12 and its G-protein-coupled receptor CXCR4.The Journal of biological chemistry · 2009Article
- Structure of the calcineurin-NFAT complex: defining a T cell activation switch using solution NMR and crystal coordinates.Structure (London, England : 1993) · 2007Article
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7 authors.
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Abstract
Cross-saturation experiments allow the identification of the contact residues of large protein complexes (MW>50 K) more rigorously than conventional NMR approaches which involve chemical shift perturbations and hydrogen-deuterium exchange experiments [Takahashi et al. (2000) Nat. Struct. Biol., 7, 220-223]. In the amide proton-based cross-saturation experiment, the combined use of high deuteration levels for non-exchangeable protons of the ligand protein and a solvent with a low concentration of (1)H(2)O greatly enhanced the selectivity of the intermolecular cross-saturation phenomenon. Unfortunately, experimental limitations caused losses in sensitivity. Furthermore, since main chain amide protons are not generally exposed to solvent, the efficiency of the saturation transfer directed to the main chain amide protons is not very high. Here we propose an alternative cross-saturation experiment which utilizes the methyl protons of the side chains of the ligand protein. Owing to the fast internal rotation along the methyl axis, we theoretically and experimentally demonstrated the enhanced efficiency of this approach. The methyl-utilizing cross-saturation experiment has clear advantages in sensitivity and saturation transfer efficiency over the amide proton-based approach.
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