Intrinsically disordered proteins (IDPs), proteins that lack a uniquely folded structure, comprise a significant portion of eukaryotic proteomes and play essential roles in signal transduction and cell cycle control. Mapping the dynamics and conformational ensembles of these proteins is essential to understanding their function. IDPs are generally thought to bind via coupled folding and binding. Sic1, however, even in its bound state with Cdc4, remains largely disordered and ‘ultrasensitive’. The lack of static structure and dynamic nature of this process poses challenges for many traditional biophysical techniques, highlighting the importance of computational methods for its characterization. Molecular dynamics (MD) simulations of IDPs are often complicated by biases introduced by force fields originally optimized to simulate folded proteins. Often simulations oversample secondary structure and lead to collapsed protein conformations. This study aims to consider canonical MD force fields and simulation methods and how accurately these techniques are able to reproduce experimental results. We carried out simulations in both implicit and explicit (with varying salt concentration) solvents with the force fields Amber12, Charmm27, OPLS-AA and Gromos at multiple temperatures. Simulations in implicit solvent were not able to recapitulate experimental structural data and always led to collapsed structures. Simulations in explicit solvents (TIP3P, TIP4P and SPC water models were used where appropriate for force field) achieved more native-like states, however some still led to collapse. Salt concentration had a strong impact on the compactness of the protein providing clues into the source of non-native compactness in MD simulations of IDPs.