Despite great advances in experimental methods for protein structure determination, the unambiguous characterization of multiple conformational states remains a challenge. Difficulties primarily arise from the huge range of structures that proteins can assume and technical limitations preventing rapid sampling of physiologically relevant conformers. Integrative structural biology combines structural information coming from multiple experimental sources, thus compensating for technique-specific shortcomings that result in data that is noisy, ambiguous, and/or unevenly distributed. In MeilerLab, we developed ConfChangeMover, an ad-hoc method within the Rosetta software suite capable to exploit sparse or ambiguous structural constraints to move proteins from a known conformation toward a new functional state (In publication).