Abstract
Inomata et al. suggested that protein folding of ubiquitin in HeLa cells is destabilised, partly due to interactions with endogenous interacting proteins. This result was a challenge to the general belief that protein folding inside cells is stabilised through macromolecular crowding and macromolecular confinement effects. Later, in vitro NMR experiments demonstrated that protein crowders can be mildly destabilising proteins by non-specific interactions, which was confirmed by recent molecular dynamics simulation studies. Here we briefly review these recent findings on the relationship between protein structure, dynamics and stability in intracellular environments.
