Equation 10 · Part 1 · Structure from Sequence: What Protein Folding Prediction Did and Did Not Settle
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with single-site fields and pair couplings fitted so that the model reproduces the single-column and pairwise frequencies of the alignment. Marks and colleagues reported that the strength of the inferred couplings is a strong predictor of residue proximity in the folded structure, and that the top-scoring couplings are accurate and well-distributed enough to define a three-dimensional fold [ 5 ] . Morcos and colleagues developed a computationally efficient direct-coupling analysis that disentangled direct from indirect correlations and evaluated contact-prediction accuracy across a large number of protein domain families from sequence information alone [ 6 ] .
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Sources cited in the surrounding passage
- [5] Protein 3D Structure Computed from Evolutionary Sequence Variation ↗
- [6] Direct-coupling analysis of residue coevolution captures native contacts across many protein families ↗
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