AI scientist systems increasingly choose biological foundation models before they choose experiments. In protein pipelines, this creates a concrete engineering and scientific question: when is the cost of structural inference worth paying over a cheaper sequence-only model? We introduce the information bonus (IB), a task-level metric that measures the linearly accessible advantage of frozen single-sequence AlphaFold2 Evoformer representations over frozen ESM-2 embeddings under protein-level cross-validation. Across binding affinity regression (PDBbind, n=5,680), conformational flexibility (ATLAS molecular dynamics, 268 proteins), and allosteric-site classification (AlloSigDB, n=9,925 residues), IB is sharply mechanism-dependent. ESM-2 dominates binding affinity (IB=-0.141; Pearson r=0.449 vs. 0.307) and binary flexibility (IB=-0.060; AUROC 0.824 vs. 0.764; p=0.0017). AF2 single representations give the only above-chance allostery predictions (IB=+0.064; AUROC 0.548 vs. 0.485), revealing long-range geometric signal not recovered from sequence alone. We also identify a residue-level leakage artifact: naive residue splits inflate RMSF performance by 27-39% depending on the representation, enough to reverse representation rankings. These results turn representation selection into a measurable decision for AI-for-science systems.

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