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• W2017698487 abstract "We use NMR spectra to determine protein-protein contact sites by observing differences in amide proton hydrogen-deuterium exchange in the complex compared to the free protein in solution. Aprotic organic solvents are used to preserve H/D labeling patterns that would be scrambled in water solutions. The binding site between the mammalian co-chaperone Aha1 with the middle domain of the chaperone Hsp90 obtained by our H/D exchange method corresponds well with that in the X-ray crystal structure of the homologous complex from yeast, even to the observation of a secondary binding site. This method can potentially provide data for complexes with unknown structure and for large or dynamic complexes inaccessible via NMR and X-ray methods." @default.
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• W2017698487 date "2008-04-07" @default.
• W2017698487 modified "2023-09-25" @default.
• W2017698487 title "Hydrogen-deuterium exchange strategy for delineation of contact sites in protein complexes" @default.
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• W2017698487 doi "https://doi.org/10.1016/j.febslet.2008.03.043" @default.
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