Supplementary Figure 7: Time-resolved anisotropies and FRET.
From: Precision and accuracy of single-molecule FRET measurements—a multi-laboratory benchmark study
The time-resolved anisotropies of dyes bound to a larger object (e.g. DNA or protein) normally consist of a fast decay from rotational relaxation of the dipole (left) and of a slow decay from translational relaxation (right). τET = 1/kFRET: time of energy transfer; rA,∞: residual anisotropy of dye A. (Figure from ref. 1). The data exemplarily shown is from a single measurement.1 Hellenkamp, B., Wortmann, P., Kandzia, F., Zacharias, M. & Hugel, T. Multidomain Structure and Correlated Dynamics Determined by Self-Consistent FRET Networks. Nat. Meth. 14, 174-180 (2017).
