https://doi.org/10.1140/epjd/e2017-70760-3
Regular Article
Monitoring methanol-induced protein unfolding by fluorescence anisotropy measurements of covalently labelled rhodamine probe*,**
1 Institut lumière matière, UMR5306 Université Claude Bernard Lyon1-CNRS, Université de Lyon, 69622 Villeurbanne Cedex, France
2 Univ Lyon, CNRS, Université Claude Bernard Lyon 1, Ens de Lyon, Institut des Sciences Analytiques, UMR 5280, 5 rue de la Doua, 69100 Villeurbanne, France
a
e-mail: rodolphe.antoine@univ-lyon1.fr
Received: 6 December 2016
Received in final form: 3 April 2017
Published online: 9 June 2017
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.
Contribution to the Topical Issue “Dynamics of Systems at the Nanoscale”, edited by Andrey Solov’yov and Andrei Korol.
Supplementary material in the form of one pdf file available from the Journal web page at https://doi.org/10.1140/epjd/e2017-70760-3
© EDP Sciences, Società Italiana di Fisica, Springer-Verlag 2017
