Understanding the mechanisms underlying biological function in proteins relies on the ability to characterize their conformational structure, which remains challenging for multidomain proteins. Here, the authors introduce a protocol (QEBSS) that combines molecular dynamics simulations and nuclear magnetic resonance data to find experimentally validated conformational ensembles of flexible multidomain proteins, and demonstrate its advantages by applying it to study the dynamics of calmodulin, EN2, MANF, and CDNF.
- Amanda E. Sandelin
- Ricky Nencini
- O. H. Samuli Ollila
