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• W2915030161 endingPage "817" @default.
• W2915030161 startingPage "807" @default.
• W2915030161 abstract "pH is an important factor that affects the protein structure, stability, and activity. Here, we probe the nature of the low-pH structural form of the homodimeric CcdB (controller of cell death B) protein. Characterization of CcdB protein at pH 4 and 300 K using circular dichroism spectroscopy, 8-anilino-1-naphthalene-sulphonate binding, and Trp solvation studies suggests that it forms a partially unfolded state with a dry core at equilibrium under these conditions. CcdB remains dimeric at pH 4 as shown by multiple techniques, such as size-exclusion chromatography coupled to multiangle light scattering, analytical ultracentrifugation, and electron paramagnetic resonance. Comparative analysis using two-dimensional 15N-1H heteronuclear single-quantum coherence NMR spectra of CcdB at pH 4 and 7 suggests that the pH 4 and native state have similar but nonidentical structures. Hydrogen-exchange-mass-spectrometry studies demonstrate that the pH 4 state has substantial but anisotropic changes in local stability with core regions close to the dimer interface showing lower protection but some other regions showing higher protection relative to pH 7." @default.
• W2915030161 created "2019-02-21" @default.
• W2915030161 creator A5006552242 @default.
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• W2915030161 creator A5087190887 @default.
• W2915030161 date "2019-03-01" @default.
• W2915030161 modified "2023-10-12" @default.
• W2915030161 title "CcdB at pH 4 Forms a Partially Unfolded State with a Dry Core" @default.
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• W2915030161 doi "https://doi.org/10.1016/j.bpj.2019.01.026" @default.
• W2915030161 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6401195" @default.
• W2915030161 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30777307" @default.
• W2915030161 hasPublicationYear "2019" @default.
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