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pubmed-article:18316034pubmed:abstractTextSite-directed spin labeling electron paramagnetic resonance methods have been an important tool in studying protein-protein interactions. Labels are often attached to a cysteine residue, and spectra are acquired with and without binding partner(s) to provide information on the binding. This requires a knowledge of the label location which is simplified if the label remains faithfully attached to the designated residue in the complex. We report a system where this is not the case because the label was extracted by dialysis-resistant glutathione molecules. Once this artifact is identified, spectral subtraction provides a solution for meaningful data interpretation.lld:pubmed
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pubmed-article:18316034pubmed:authorpubmed-author:FungL W-MLWlld:pubmed
pubmed-article:18316034pubmed:authorpubmed-author:AntoniouChloe...lld:pubmed
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pubmed-article:18316034pubmed:dateRevised2009-11-18lld:pubmed
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pubmed-article:18316034pubmed:articleTitlePotential artifacts in using a glutathione S-transferase fusion protein system and spin labeling electron paramagnetic resonance methods to study protein-protein interactions.lld:pubmed
pubmed-article:18316034pubmed:affiliationDepartment of Chemistry, University of Illinois at Chicago, 845 West Taylor Street, MC 111, Chicago, IL 60607, USA.lld:pubmed
pubmed-article:18316034pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:18316034pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
pubmed-article:18316034pubmed:publicationTypeResearch Support, N.I.H., Extramurallld:pubmed
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