Protein folding is a fascinating, not fully understood phenomenon in biology. Molecular dynamics (MD) simulations are an invaluable tool to study conformational changes at atomistic detail, including unfolding processes of proteins. However, the accuracy of the conformational ensembles derived from MD simulations inevitably rely on the quality of the underlying force field in combination with the respective water model. Here, we investigate protein folding, unfolding and misfolding of fast folding proteins by examining different force fields with their recommended water models, i.e., ff14SB with the TIP3P model and ff19SB with the OPC model. To this end, we generated long conventional MD simulations highlighting perks and pitfalls of these setups. Using Markov State Models, we defined kinetically independent conformational substates and emphasized their distinct characteristics as well as their corresponding state probabilities. Surprisingly, we found substantial differences in thermodynamics and kinetics of protein folding, depending on the combination of protein force field and water model, originating primarily from the different water models. These results emphasize the importance of carefully choosing the force field and the respective water model, as they determine the accuracy of the observed dynamics and folding events. Thus, the findings support the hypothesis that the water model is equally important as the force field hence need to be considered in future studies investigating protein dynamics and folding in all areas of biophysics. Here, we provide the trajectories used to study protein folding of Chignolin and CLN025.