In this work, we have used an MSM approach to systematically analyze the essential conformational dynamics of the 10-residue β-hairpin miniprotein chignolin, identifying the relevant macroscopic conformational states (native, misfolded, and unfolded) that define the folding landscape. From over 200 µs of aggregate trajectory data obtained in nine different force fields (AMBER14SB, AMBER99, AMBER99SB, AMBER99SB-ildn, AMBER99SBnmr1ildn, CHARMM22*, CHARMM27, CHARMM36 and OPLS-aa), we constructed MSMs and compared the results against experiment using a reduced chi-squared metric. Performance varied widely across the nine force fields, but several displayed reasonable agreement with the measured native state population and NMR chemical shifts and J-coupling constants.