It has been a long-standing and intriguing issue to develop robust methods to identify metastable states and interstate transitions from simulations or experimental data to understand the functional conformational changes of proteins. It is usually hard to define the complicated boundaries of the states in the conformational space using most of the existing methods, and they often lead to parameter-sensitive results. Here, we present a new approach, visualized Trajectory Map (vTM), to identify the metastable states and the rare interstate transitions, by considering both the conformational similarity and the temporal successiveness of conformations. The vTM is able to give a nonambiguous description of slow dynamics. The case study of a beta-hairpin peptide shows that the vTM can reveal the states and transitions from all-atom MD trajectory data even when a single observable (i.e, one-dimensional reaction coordinate) is used. We also use the vTM to refine the folding/unfolding mechanism of HP35 in explicit water by analyzing a 125 mu s all-atom MD trajectory and obtain folding/unfolding rates of about 1/mu s, which are in good agreement with the experimental values.