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Updated: May 15, 2026

Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
Published on: November 28, 2017
Detection of Noncovalent Protein-Ligand Complexes of D-DT Variants by MALDI-TOF Mass Spectrometry
Andrew Parkins1, Georgios Pantouris1, Andreas H Franz2
1Department of Chemistry, University of the Pacific, Stockton, CA, 95211, USA.
Abstract:
Mass spectrometry (MS) is the analytical technique of choice when information about molecular mass and structural characteristics of minute sample quantities are desired. Here, we report a generally applicable, robust, and fast method for sample preparation and matrix-assisted laser desorption/ionization (MALDI)-time-of-flight (TOF) analysis of D-dopachrome tautomerase (D-DT or MIF-2) in the presence of a small molecule ligand. We show that noncovalent protein-ligand complexes can be detected. Our method will allow researchers to quickly screen large libraries of ligands against a given protein target and should be considered a supplement to other detection techniques for noncovalent protein-ligand complexes.
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