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Updated: Aug 16, 2026

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
Published on: October 15, 2018
The contact interface of a 120 kD CheA-CheW complex by methyl TROSY interaction spectroscopy
Damon J Hamel1, Frederick W Dahlquist
1Department of Chemistry and Biochemistry, University of California Santa Barbara, California 93106, USA.
Abstract:
During bacterial chemotaxis, the histidine autokinase CheA interacts with the chemotaxis receptors with the help of the coupling protein CheW. This interaction is typical of many macromolecular complexes where protein-protein interactions play an important role. In this case, a relatively small protein, CheW, becomes part of a much larger complex. Here we describe a new method to map the residues at a protein-protein interface for macromolecular complexes of molecular weight greater than 100 kD.
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