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Default NMR probing of protein-protein interactions using reporter ligands and affinity tags.

NMR probing of protein-protein interactions using reporter ligands and affinity tags.

Related Articles NMR probing of protein-protein interactions using reporter ligands and affinity tags.

J Am Chem Soc. 2004 Feb 18;126(6):1636-7

Authors: Ludwiczek ML, Baminger B, Konrat R

A novel method is proposed for the detection and quantification of protein-protein interactions in solution. In this approach, one protein binding partner is tagged with a ligand binding domain, and protein-protein interaction is monitored via changes in the NMR relaxation of a reporter ligand which reversibly binds to the ligand binding domain. The particular benefit of the method is that only minute amounts of protein material and no isotope labeling are required. Its ease of implementation and the high-throughput capabilities make the method an attractive complement to existing proteomic methodology.

PMID: 14871086 [PubMed - indexed for MEDLINE]



Source: PubMed
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