{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Shen Y"],"funding":["National Institute of Diabetes and Digestive and Kidney Diseases"],"pagination":["146-158"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5734315"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["27(1)"],"pubmed_abstract":["Using fine-tuned hydrogen bonding criteria, a library of coiled peptide fragments has been generated from a large set of high-resolution protein X-ray structures. This library is shown to be an improved representation of ϕ/ψ torsion angles seen in intrinsically disordered proteins (IDPs). The ϕ/ψ torsion angle distribution of the library, on average, provides good agreement with experimentally observed chemical shifts and <sup>3</sup> J<sub>HN-Hα</sub> coupling constants for a set of five disordered proteins. Inspection of the coil library confirms that nearest-neighbor effects significantly impact the ϕ/ψ distribution of residues in the coil state. Importantly, <sup>3</sup> J<sub>HN-Hα</sub> coupling constants derived from the nearest-neighbor modulated backbone ϕ distribution in the coil library show improved agreement to experimental values, thereby providing a better way to predict <sup>3</sup> J<sub>HN-Hα</sub> coupling constants for IDPs, and for identifying locations that deviate from fully random behavior."],"journal":["Protein science : a publication of the Protein Society"],"pubmed_title":["Prediction of nearest neighbor effects on backbone torsion angles and NMR scalar coupling constants in disordered proteins."],"pmcid":["PMC5734315"],"funding_grant_id":["DK029046‐10"],"pubmed_authors":["Roche J","Bax A","Shen Y","Grishaev A"],"additional_accession":[]},"is_claimable":false,"name":"Prediction of nearest neighbor effects on backbone torsion angles and NMR scalar coupling constants in disordered proteins.","description":"Using fine-tuned hydrogen bonding criteria, a library of coiled peptide fragments has been generated from a large set of high-resolution protein X-ray structures. This library is shown to be an improved representation of ϕ/ψ torsion angles seen in intrinsically disordered proteins (IDPs). The ϕ/ψ torsion angle distribution of the library, on average, provides good agreement with experimentally observed chemical shifts and <sup>3</sup> J<sub>HN-Hα</sub> coupling constants for a set of five disordered proteins. Inspection of the coil library confirms that nearest-neighbor effects significantly impact the ϕ/ψ distribution of residues in the coil state. Importantly, <sup>3</sup> J<sub>HN-Hα</sub> coupling constants derived from the nearest-neighbor modulated backbone ϕ distribution in the coil library show improved agreement to experimental values, thereby providing a better way to predict <sup>3</sup> J<sub>HN-Hα</sub> coupling constants for IDPs, and for identifying locations that deviate from fully random behavior.","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Jan","modification":"2024-11-09T07:47:57.678Z","creation":"2019-03-26T22:26:18Z"},"accession":"S-EPMC5734315","cross_references":{"pubmed":["28884933"],"doi":["10.1002/pro.3292"]}}