While autoinhibited architectures of talin are known from cryo-electron microscopy, its behaviour in solution has remained underexplored. Here, the authors use size-exclusion chromatography coupled with in-line small-angle X-ray scattering, Monte Carlo modeling and AlphaFold predictions to determine the conformational landscape of full-length talin in solution, showing that this cytoplasmic adapter protein does not adopt a single compact structure but instead populates a broad, flexible conformational ensemble characterized by R3 subdomain repositioning and partial F3-R9 subdomain disengagement.
- Bright Shi
- Gilbert Reyes
- Zimei Bu
