Structural innovation in proteins is constrained by past selection for mutational robustness

Natural protein structures show a narrow mutational profile with high mutational robustness but limited structural variation, unlike RNA, when secondary-structure distributions are compared under point mutations.

• Why it matters: The key gap is how different chemical alphabets shape the evolution of functional structures, and whether robustness constraints limit innovation in proteins versus RNA.
• What they did: The study used RNAfold and ESMFold to predict secondary-structure changes from point mutations, then integrated structure prediction with phylogenetic data and simulations.
• The result: Protein robustness is linked to selection that buffers translation errors, and this comes with reduced propensity for structural innovation in proteins.

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