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Mass spectrometry can be used to characterize multiprotein complexes, defining their subunit stoichiometry and composition following solution disruption and collision-induced dissociation (CID). While CID of protein complexes in the gas phase typically results in the dissociation of unfolded subunits, a second atypical route is possible wherein compact subunits or subcomplexes are ejected without unfolding. Because tertiary structure and subunit interactions may be retained, this is the preferred route for structural investigations. How can we influence which pathway is adopted? By studying properties of a series of homomeric and heteromeric protein complexes and varying their overall charge in solution, we found that low subunit flexibility, higher charge densities, fewer salt bridges, and smaller interfaces are likely to be involved in promoting dissociation routes without unfolding. Manipulating the charge on a protein complex therefore enables us to direct dissociation through structurally informative pathways that mimic those followed in solution.

Original publication

DOI

10.1016/j.str.2013.06.004

Type

Journal article

Journal

Structure

Publication Date

06/08/2013

Volume

21

Pages

1325 - 1337

Keywords

Animals, Crystallography, X-Ray, Humans, Molecular Dynamics Simulation, Multiprotein Complexes, Prealbumin, Protein Interaction Domains and Motifs, Protein Stability, Protein Structure, Quaternary, Protein Subunits, Protein Unfolding, Rabbits, Serum Amyloid P-Component