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Proteins in solution move subject to a complex superposition of global translational and rotational diffusion as well as internal relaxations covering a wide range of time scales.With the advent of new high-flux neutron spectrometers in combination with enhanced analysis frameworks it has become possible to separate these different contributions. We discuss new approaches to the analysis by presenting example spectra and fits from data recorded on the backscattering spectrometers IN16, IN16B, and BASIS on the same protein solution sample.We illustrate the separation of the rotational and translational diffusion contribution, the accurate treatment of the solvent contribution, and the extraction of information on internal fluctuations. We also exemplify the progress made in passing from second- to third-generation backscattering spectrometers. [ABSTRACT FROM AUTHOR]