ArticleBiochemistry2016
Positioning the Intracellular Salt Potassium Glutamate in the Hofmeister Series by Chemical Unfolding Studies of NTL9.
Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed.
- Destabilization of the D2 domain of Thermotoga maritima arginine binding protein induced by guanidinium thiocyanate and its counteraction by stabilizing agents.Protein science : a publication of the Protein Society · 2024Article
- On the Stabilizing Effect of Aspartate and Glutamate and Its Counteraction by Common Denaturants.International journal of molecular sciences · 2024Article
- Solutes unmask differences in clustering versus phase separation of FET proteins.Nature communications · 2024Article
- Macromolecular Crowding, Phase Separation, and Homeostasis in the Orchestration of Bacterial Cellular Functions.Chemical reviews · 2024Review
- How Glutamate Promotes Liquid-liquid Phase Separation and DNA Binding Cooperativity of E. coli SSB Protein.Journal of molecular biology · 2022Article
- Evolution of glutamatergic signaling and synapses.Neuropharmacology · 2021Review
- General Counteraction Exerted by Sugars against Denaturants.Life (Basel, Switzerland) · 2021Article
- Potassium Glutamate and Glycine Betaine Induce Self-Assembly of the PCNA and β-Sliding Clamps.Biophysical journal · 2021Article
- The SecA ATPase motor protein binds to Escherichia coli liposomes only as monomers.Biochimica et biophysica acta. Biomembranes · 2020Article
- Stabilization of SecA ATPase by the primary cytoplasmic salt of Escherichia coli.Protein science : a publication of the Protein Society · 2019Article
- Protein Cofactors Are Essential for High-Affinity DNA Binding by the Nuclear Factor κB RelA Subunit.Biochemistry · 2018Article
- The mechanism and high-free-energy transition state of lac repressor-lac operator interaction.Nucleic acids research · 2017Article
- Glutamate promotes SSB protein-protein Interactions via intrinsically disordered regions.Journal of molecular biology · 2017Article
- The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State.Biophysical journal · 2017Article
- Basis of Protein Stabilization by K Glutamate: Unfavorable Interactions with Carbon, Oxygen Groups.Biophysical journal · 2016Article
- Protein folding on biosensor tips: folding of maltodextrin glucosidase monitored by its interactions with GroEL.The FEBS journal · 2016Article
- Molecular insights into the prototypical single-stranded DNA-binding protein fromCritical reviews in biochemistry and molecular biologyReview
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8 authors.
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Abstract
In vitro, replacing KCl with potassium glutamate (KGlu), the Escherichia coli cytoplasmic salt and osmolyte, stabilizes folded proteins and protein-nucleic acid complexes. To understand the chemical basis for these effects and rank Glu- in the Hofmeister anion series for protein unfolding, we quantify and interpret the strong stabilizing effect of KGlu on the ribosomal protein domain NTL9, relative to the effects of other stabilizers (KCl, KF, and K2SO4) and destabilizers (GuHCl and GuHSCN). GuHSCN titrations at 20 ° C, performed as a function of the concentration of KGlu or another salt and monitored by NTL9 fluorescence, are analyzed to obtain R-values quantifying the Hofmeister salt concentration (m3) dependence of the unfolding equilibrium constant K(obs) [r-value = −d ln K(obs)/dm3 = (1/RT) dΔG(obs) ° /dm3 = m-value/RT]. r-Values for both stabilizing K+ salts and destabilizing GuH+ salts are compared with predictions from model compound data. For two-salt mixtures, we find that contributions of stabilizing and destabilizing salts to observed r-values are additive and independent. At 20 ° C, we determine a KGlu r-value of 3.22 m(−1) and K2SO4, KF, KCl, GuHCl, and GuHSCN r-values of 5.38, 1.05, 0.64, −1.38, and −3.00 m(−1), respectively. The KGlu r-value represents a 25-fold (1.9 kcal) stabilization per molal KGlu added. KGlu is much more stabilizing than KF, and the stabilizing effect of KGlu is larger in magnitude than the destabilizing effect of GuHSCN. Interpretation of the data reveals good agreement between predicted and observed relative r-values and indicates the presence of significant residual structure in GuHSCN-unfolded NTL9 at 20 ° C.
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