Here, we critically compare the application combinations of two metadynamicsbased, multiple-replica sampling methods and two protein force-fields to develop a systematic understanding of the conformational ensemble of an intrinsically disordered protein. The methods chosen are bias-exchange metadynamics (BEMD) and parallel-tempering well-tempered metadynamics (PTMetaD-WTE) , which merge the advantages of PT method and metadynamics-based techniques. PTMetaD-WTE can significantly reduce the number of replicas required thanks to the potentialenergy bias introduced in the MetaD-WTE part; at the same time, the high temperature replicas from the PT part may compensate for the limited number of CVs directly biased to explore a high-dimensional phase space. On the other hand, in the BEMD method, a larger set of structural CVs is separately biased, and the system is often simulated at one temperature. Overall, the efficiency of the CV-based metadynamics methods depends on a suitable set of collective variables, which usually requires a priori knowledge of topological, chemical, and physical properties of the protein of interest.