Global Implications of Local Unfolding Phenomena, Probed by Cysteine Reactivity in Human Frataxin.
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ABSTRACT: Local events that affect specific regions of proteins are of utmost relevance for stability and function. The aim of this study is to quantitatively assess the importance of locally-focused dynamics by means of a simple chemical modification procedure. Taking human Frataxin as a working model, we investigated local fluctuations of the C-terminal region (the last 16 residues of the protein) by means of three L → C replacement mutants: L98C, L200C and L203C. The conformation and thermodynamic stability of each variant was assessed. All the variants exhibited native features and high stabilities: 9.1 (wild type), 8.1 (L198C), 7.0 (L200C) and 10.0 kcal mol-1 (L203C). In addition, kinetic rates of Cys chemical modification by DTNB and DTDPy were measured, conformational dynamics data
SUBMITTER: Faraj SE
PROVIDER: S-EPMC6370780 | biostudies-literature | 2019 Feb
REPOSITORIES: biostudies-literature
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