How robust are protein folding simulations with respect to force field parameterization?

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A general-purpose protein design framework based on mining sequence–structure relationships in known protein structures (2018, background): “may not, in fact, be capable of capturing all relevant sequence-structure effects in a single model (36).”
Simulations of interfacial processes: recent advances in force field development (2019, methodology): “The interactions between amino acids (or analogs) and graphene are described using the standard combination rules, where the amino acids (or analogs) are represented by CHARMM22* [13,18] non-polarizable”
Structure of the Bacterial Cytoskeleton Protein Bactofilin by NMR Chemical Shifts and Sequence Variation. (2016, methodology): “We used the CHARMM22* force field (33) and smoothly shifted the”
Developing a molecular dynamics force field for both folded and disordered protein states (2018, methodology): “…by previous successful efforts to reparameterize force-field torsion angles to obtain a more accurate balance between helix and coil states (10, 11, 14), we performed a similar torsion optimization targeting (AAQAA) 3 fraction helicity and polyalanine scalar couplings as described previously (14).”