ArticleAnalytical chemistry2011
Determinants of gas-phase disassembly behavior in homodimeric protein complexes with related yet divergent structures.
Article in Analytical chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed.
- Surface-induced Dissociation Mass Spectrometry as a Structural Biology Tool.Chemical reviews · 2022Review
- Predicting Protein Complex Structure from Surface-Induced Dissociation Mass Spectrometry Data.ACS central science · 2019Article
- Distinct Stabilities of the Structurally Homologous Heptameric Co-Chaperonins GroES and gp31.Journal of the American Society for Mass Spectrometry · 2019Article
- Self-assembly of toroidal proteins explored using native mass spectrometry.Chemical science · 2018Article
- Refining the Structural Model of a Heterohexameric Protein Complex: Surface Induced Dissociation and Ion Mobility Provide Key Connectivity and Topology Information.ACS central science · 2015Article
- Electron-capture dissociation and ion mobility mass spectrometry for characterization of the hemoglobin protein assembly.Protein science : a publication of the Protein Society · 2015Article
- Collision-induced release, ion mobility separation, and amino acid sequence analysis of subunits from mass-selected noncovalent protein complexes.Journal of the American Society for Mass Spectrometry · 2014Article
- Surface induced dissociation yields quaternary substructure of refractory noncovalent phosphorylase B and glutamate dehydrogenase complexes.Journal of the American Society for Mass Spectrometry · 2014Article
- The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes.Structure (London, England : 1993) · 2013Article
- The effect of a covalent and a noncovalent small-molecule inhibitor on the structure of Abg β-glucosidase in the gas-phase.Journal of the American Society for Mass Spectrometry · 2013Article
- A polymetamorphic protein.Protein science : a publication of the Protein Society · 2013Article
- The role of chaperone-subunit usher domain interactions in the mechanism of bacterial pilus biogenesis revealed by ESI-MS.Molecular & cellular proteomics : MCP · 2012Article
- Ion mobility mass spectrometry coupled with rapid protein threading predictor structure prediction and collision-induced dissociation for probing chemokine conformation and stability.Analytical chemistry · 2012Article
- Ion mobility-mass spectrometry for structural proteomics.Expert review of proteomics · 2012Review
- An electrostatic charge partitioning model for the dissociation of protein complexes in the gas phase.Journal of the American Society for Mass Spectrometry · 2011Article
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Abstract
The overall structure of a protein-protein complex reflects an intricate arrangement of noncovalent interactions. Whereas intramolecular interactions confer secondary and tertiary structure to individual subunits, intermolecular interactions lead to quaternary structure--the ordered aggregation of separate polypeptide chains into multisubunit assemblies. The specific ensemble of noncovalent contacts dictates the stability of subunit folds, enforces protein-protein binding specificity, and determines multimer stability. Consequently, noncovalent architecture is likely to play a role in the gas-phase dissociation of these assemblies during tandem mass spectrometry (MS/MS). To further advance the applicability of MS/MS to analytical problems in structural biology, a better understanding of the interplay between the structures and fragmentation behaviors of noncovalent protein complexes is essential. The present work constitutes a systematic study of model protein homodimers (bacteriophage N15 Cro, bacteriophage λ Cro, and bacteriophage P22 Arc) with related but divergent structures, both in terms of subunit folds and protein-protein interfaces. Because each of these dimers has a well-characterized structure (solution and/or crystal structure), specific noncovalent features could be correlated with gas-phase disassembly patterns as studied by collision-induced dissociation, surface-induced dissociation, and ion mobility. Of the several respects in which the dimers differed in structure, the presence or absence of intermolecular electrostatic contacts exerted the most significant influence on the gas-phase dissociation behavior. This is attributed to the well-known enhancement of ionic interactions in the absence of bulk solvent. Because salt bridges are general contributors to both intermolecular and intramolecular stability in protein complexes, these observations are broadly applicable to aid in the interpretation or prediction of dissociation spectra for noncovalent protein assemblies.
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