ArticleProtein science : a publication of the Protein Society2017
Protein charge determination and implications for interactions in cell extracts.
Article in Protein science : a publication of the Protein Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 20 citations in OpenAlex.
- The iron metalloproteome of Pseudomonas aeruginosa under oxic and anoxic conditions.Metallomics : integrated biometal science · 2025Article
- Site Identification by Ligand Competitive Saturation-Biologics Approach for Structure-Based Protein Charge Prediction.Molecular pharmaceutics · 2023Article
- Single-Protein Identification by Simultaneous Size and Charge Imaging Using Evanescent Scattering Microscopy.ACS sensors · 2022Article
- IgG Charge: Practical and Biological Implications.Antibodies (Basel, Switzerland) · 2019Article
- Review
- Subcellular stoichiogenomics reveal cell evolution and electrostatic interaction mechanisms in cytoskeleton.BMC genomics · 2018Article
- Surface Charge Modulates Protein-Protein Interactions in Physiologically Relevant Environments.Biochemistry · 2018Article
- Quinary interactions with an unfolded state ensemble.Protein science : a publication of the Protein Society · 2017Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Decades of dilute-solution studies have revealed the influence of charged residues on protein stability, solubility and stickiness. Similar characterizations are now required in physiological solutions to understand the effect of charge on protein behavior under native conditions. Toward this end, we used free boundary and native gel electrophoresis to explore the charge of cytochrome c in buffer and in Escherichia coli extracts. We find that the charge of cytochrome c was ∼2-fold lower than predicted from primary structure analysis. Cytochrome c charge was tuned by sulfate binding and was rendered anionic in E. coli extracts due to interactions with macroanions. Mutants in which three or four cationic residues were replaced with glutamate were charge-neutral and "inert" in extracts. A comparison of the interaction propensities of cytochrome c and the mutants emphasizes the role of negative charge in stabilizing physiological environments. Charge-charge repulsion and preferential hydration appear to prevent aggregation. The implications for molecular organization in vivo are discussed.
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Registered trials
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