{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,11]],"date-time":"2025-11-11T13:05:51Z","timestamp":1762866351995},"reference-count":37,"publisher":"Oxford University Press (OUP)","issue":"12","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2014,6,15]]},"abstract":"<jats:p>Motivation: Accurately predicting protein side-chain conformations is an important subproblem of the broader protein structure prediction problem. Several methods exist for generating fairly accurate models for moderate-size proteins in seconds or less. However, a major limitation of these methods is their inability to model post-translational modifications (PTMs) and unnatural amino acids. In natural living systems, the chemical groups added following translation are often critical for the function of the protein. In engineered systems, unnatural amino acids are incorporated into proteins to explore structure\u2013function relationships and create novel proteins.<\/jats:p>\n               <jats:p>Results: We present a new version of SIDEpro to predict the side chains of proteins containing non-standard amino acids, including 15 of the most frequently observed PTMs in the Protein Data Bank and all types of phosphorylation. SIDEpro uses energy functions that are parameterized by neural networks trained from available data. For PTMs, the and accuracies are comparable with those obtained for the precursor amino acid, and so are the RMSD values for the atoms shared with the precursor amino acid. In addition, SIDEpro can accommodate any PTM or unnatural amino acid, thus providing a flexible prediction system for high-throughput modeling of proteins beyond the standard amino acids.<\/jats:p>\n               <jats:p>Availability and implementation: SIDEpro programs and Web server, rotamer libraries and data are available through the SCRATCH suite of protein structure predictors at http:\/\/scratch.proteomics.ics.uci.edu\/<\/jats:p>\n               <jats:p>Contact: \u00a0pfbaldi@uci.edu<\/jats:p>\n               <jats:p>Supplementary information: \u00a0Supplementary Data are available at Bioinformatics online.<\/jats:p>","DOI":"10.1093\/bioinformatics\/btu106","type":"journal-article","created":{"date-parts":[[2014,2,27]],"date-time":"2014-02-27T01:26:41Z","timestamp":1393464401000},"page":"1681-1689","source":"Crossref","is-referenced-by-count":7,"title":["Incorporating post-translational modifications and unnatural amino acids into high-throughput modeling of protein structures"],"prefix":"10.1093","volume":"30","author":[{"given":"Ken","family":"Nagata","sequence":"first","affiliation":[{"name":"1 \u00a01Department of Computer Science and 2Institute for Genomics and Bioinformatics, University of California, Irvine, CA, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Arlo","family":"Randall","sequence":"additional","affiliation":[{"name":"1 \u00a01Department of Computer Science and 2Institute for Genomics and Bioinformatics, University of California, Irvine, CA, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Pierre","family":"Baldi","sequence":"additional","affiliation":[{"name":"1 \u00a01Department of Computer Science and 2Institute for Genomics and Bioinformatics, University of California, Irvine, CA, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2014,2,25]]},"reference":[{"key":"2023012711064342300_btu106-B1","doi-asserted-by":"crossref","first-page":"760","DOI":"10.1021\/ci100223t","article-title":"Data-driven high-throughput prediction of the 3-D structure of small molecules: review and progress","volume":"51","author":"Andronico","year":"2011","journal-title":"J. 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