{"ID":6250170,"CreatedAt":"2026-07-09T21:19:31.300590468Z","UpdatedAt":"2026-07-09T21:19:31.300590468Z","DeletedAt":null,"paper_url":"https://arxiv.org/abs/1207.2484","arxiv_id":"1207.2484","title":"Using Sequence Alignments to Predict Protein Structure and Stability With High Accuracy","abstract":"We present a sequence-based probabilistic formalism that directly addresses co-operative effects in networks of interacting positions in proteins, providing significantly improved contact prediction, as well as accurate quantitative prediction of free energy changes due to non-additive effects of multiple mutations. In addition to these practical considerations, the agreement of our sequence-based calculations with experimental data for both structure and stability demonstrates a strong relation between the statistical distribution of protein sequences produced by natural evolutionary processes, and the thermodynamic stability of the structures to which these sequences fold.","url_abs":"https://arxiv.org/abs/1207.2484v1","url_pdf":"https://arxiv.org/pdf/1207.2484v1","authors":"Alan Lapedes, Bertrand Giraud, Christopher Jarzynski","published":"2012-07-10T20:24:42Z","has_code":false}