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FEBS Lett. 2008 Apr 30;582(10):1495-500. doi: 10.1016/j.febslet.2008.03.043. Epub 2008 Apr 7.

Hydrogen-deuterium exchange strategy for delineation of contact sites in protein complexes.

Author information

  • 1Department of Molecular Biology MB2, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, United States. dyson@scripps.edu

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.

PMID:
18396165
PMCID:
PMC2440508
DOI:
10.1016/j.febslet.2008.03.043
[PubMed - indexed for MEDLINE]
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