Monitoring methanol-induced protein unfolding by fluorescence anisotropy measurements of covalently labelled rhodamine probe
Résumé
We describe the use of an extrinsic fluorophore (Rhodamine B isothiocyanate) as a versatile probe to measure rotational motions of proteins. To illustrate the usefulness of this probe, we describe the fluorescence anisotropy values of this fluorophore covalently linked to myoglobin protein measured in aqueous solutions of increased methanol content. Methanol-induced unfolding is revealed by the transition from constrained to free rotation of the covalently attached rhodamine B fluorophore. Graphical abstract Constrained to Free a) b) MGLSDGEWQQVLNVWGKVEA DIAGHGQEVLIRLFTGHPET LEKFDKFKHLKTEAEMKASE DLKKHGTVVLTALGGILKKK GHHEAELKPLAQSHATKHKI PIKYLEFISDAIIHVLHSKH PGDFGADAQGAMTKALELFR NDIAAKYKELGFQG 2 Introduction:
Domaines
Chimie analytiqueOrigine | Fichiers produits par l'(les) auteur(s) |
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