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Protein structures can now be predicted and designed at scale, yet experimental access to dynamics and conformational heterogeneity remains limited in throughput. This gap prevents a systematic understanding of how protein sequences encode motion and functional flexibility. Here, we establish a scalable experimental pipeline combining protein design, automated production, and nuclear magnetic resonance (NMR) spectroscopy to enable high-throughput characterization of protein structure and dynamics at atomic resolution. A single operator can produce and analyze hundreds of isotopically labeled proteins per week, with per-sample cost largely defined by DNA synthesis. To benchmark this approach, we experimentally characterized 384 de novo designed proteins spanning diverse regions of structure space. High-quality two-dimensional NMR spectra were obtained for 239 samples (62% of designs overall). NMR characterization confirmed that the designed proteins adopt their intended folds, and revealed unexpected local dynamics that are not captured by current computational models. Our approach establishes a foundation for data-driven modelling of sequence–structure–dynamics relationships and unlocks a new regime of statistical structural biology, where insight into protein biophysics is gained from experimental ensemble studies of suitably designed protein clusters.