Abstract
Identification of the interfaces of large (Mr > 50,000) protein–protein complexes in solution by high resolution NMR has typically been achieved using experiments involving chemical shift perturbation and/or hydrogen-deuterium exchange of the main chain amide groups of the proteins. Interfaces identified using these techniques, however, are not always identical to those revealed using X-ray crystallography. In order to identify the contact residues in a large protein–protein complex more accurately, we developed a novel NMR method that uses cross-saturation phenomena in combination with TROSY detection in an optimally deuterium labeled system.
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Acknowledgements
We thank F. Delaglio for providing scripts for spectra analysis and M. Nakasako for useful discussions.
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Takahashi, H., Nakanishi, T., Kami, K. et al. A novel NMR method for determining the interfaces of large protein–protein complexes. Nat Struct Mol Biol 7, 220–223 (2000). https://doi.org/10.1038/73331
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DOI: https://doi.org/10.1038/73331
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