OmeDDG: Improved Protein Mutation Stability Prediction Based on Predicted 3D Structures
Determining changes in the protein’s thermal stability following mutations is critical in protein engineering and understanding pathogenic missense mutations. Despite the development of various computational methods to predict the effects of single-point mutations, their accuracy remains limited. In...
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Veröffentlicht in: | The journal of physical chemistry. B 2024-01, Vol.128 (1), p.67-76 |
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