Utilization of Methyl Proton Resonances in Cross-Saturation Measurement for Determining the Interfaces of Large Protein–Protein Complexes

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Journal of Biomolecular NMR, Vol. 34, Iss. 3, 2006-03 ,pp. : 167-177

Springer Publishing Company

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Electrostatically-driven fast association and perdeuteration allow detection of transferred cross-relaxation for G protein-coupled receptor ligands with equilibrium dissociation constants in the high-to-low nanomolar range

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Structure of the CAP-DNA Complex at 2.5 A Resolution: A Complete Picture of the Protein-DNA Interface

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Adiabatic-passage cross polarization in N-15 NMR spectroscopy of peptides weakly associated to phospholipids: Determination of large RDC

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Nonglucosylated oligosaccharides are transferred to protein in MI8-5 Chinese hamster ovary cells

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