CcdB at pH 4 Forms a Partially Unfolded State with a Dry Core.

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 spectr

SUBMITTER: Baliga C 

PROVIDER: S-EPMC6401195 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature