Figure 1: Complementarity between SEFs and physics-based energy functions. | Nature Communications

Figure 1: Complementarity between SEFs and physics-based energy functions.

From: Protein design with a comprehensive statistical energy function and boosted by experimental selection for foldability

Figure 1

(a) Sequence identities between native proteins, proteins designed with SEF, proteins designed with SEF_v and proteins obtained with Rosetta fixed backbone design (Ros_fb). Results are averages over 40 target proteins. (b) Fractions of highly target-like models in structures predicted ab initio using native and using different designed sequences. The fold classes of targets are indicated. For each fold class, results are averages over ten targets. (c) Energies of designed sequences relative to corresponding native sequences for 40 target proteins of different fold classes. The energies were calculated with ESEF. (d) Same as in c, but the energies were calculated with Rosetta.

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