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. Author manuscript; available in PMC: 2018 Feb 1.
Published in final edited form as: SLAS Discov. 2016 Oct 22;22(2):176–186. doi: 10.1177/1087057116674312

Figure 1. FRET-based HTS-compatible system to monitor RyR interaction with CaM and FKBP.

Figure 1

(A) Schematic illustration of the FKBP and CaM binding locations within the RyR cryo-EM map (16,17), and donor and acceptor label positions on ribbon-structures of FKBP and CaM, respectively (PDB 4IQ2 and 2BCX). (B) Time-resolved (TR) fluorescence waveforms yield the fluorescence lifetime (FLT) readout that enables high-precision measurements of FRET between D-FKBP and A-CaM. FRET is calculated as the fractional change between the fluorescence lifetimes of donor-only and donor+acceptor sample lifetime (τD and τDA, respectively). (C) FRET changes can be due to alterations in FKBP or CaM binding affinity and/or RyR structure that affects distance relationships between fluorophores.