In recent years the analysis of molecular dynamics trajectories using dimensionality reduction algorithms has become commonplace. These algorithms seek to find a low-dimensional representation of a trajectory that is, according to a well-defined criterion, optimal. A number of different strategies for generating projections of trajectories have been proposed but little has been done to systematically compare how these various approaches fare when it comes to analysing trajectories for biomolecules in explicit solvent. In the following paper, we have thus analyzed a molecular dynamics trajectory of the C-terminal fragment of the immunoglobulin binding domain B1 of protein G of Streptococcus modelled in explicit solvent using a range of different dimensionality reduction algorithms. We have then tried to systematically compare the projections generated using each of these algorithms by using a clustering algorithm to find the positions and extents of the basins in the high-dimensional energy landscape. We find that no algorithm outshines all the other in terms of the quality of the projection it generates. Instead, all the algorithms do a reasonable job when it comes to building a projection that separates some of the configurations that lie in different basins. Having said that, however, all the algorithms struggle to project the basins because they all have a large intrinsic dimensionality.