Coarse-grained molecular dynamics simulations allow for the modeling of increasingly complex systems. A recent example is the modeling of an entire cell 2 in the Martini 3 force field with a full interior of molecular components with proteins comprising as much as 40 % of the intracellular volume. However, folded proteins in Martini 3 (version 3.0.0) are not yet stable without the application of external bias potentials, like elastic networks or Gō-like models. Furthermore, additional secondary structure-specific potentials (defined using the DSSP algorithm ), need to be employed to limit fold-breaking fluctuations, however, these also restrict the modeling of conformational changes and transient folds, which are often desired in computational studies of proteins.