{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Jonker HRA"],"funding":["Deutsche Forschungsgemeinschaft","Hessisches Ministerium für Wissenschaft und Kunst"],"pagination":["20659-20665"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7692951"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["59(46)"],"pubmed_abstract":["Despite the great interest in glycoproteins, structural information reporting on conformation and dynamics of the sugar moieties are limited. We present a new biochemical method to express proteins with glycans that are selectively labeled with NMR-active nuclei. We report on the incorporation of <sup>13</sup> C-labeled mannose in the C-mannosylated UNC-5 thrombospondin repeat. The conformational landscape of the C-mannose sugar puckers attached to tryptophan residues of UNC-5 is characterized by interconversion between the canonical <sup>1</sup> C<sub>4</sub> state and the B<sub>03</sub> / <sup>1</sup> S<sub>3</sub> state. This flexibility may be essential for protein folding and stabilization. We foresee that this versatile tool to produce proteins with selectively labeled C-mannose can "],"journal":["Angewandte Chemie (International ed. in English)"],"pubmed_title":["NMR Spectroscopic Characterization of the C-Mannose Conformation in a Thrombospondin Repeat Using a Selective Labeling Approach."],"pmcid":["PMC7692951"],"funding_grant_id":["FOR 2509","BMRZ"],"pubmed_authors":["Jonker HRA","Bakker H","Tiemann B","Schwalbe H","Shcherbakova A","Saxena K"],"additional_accession":[]},"is_claimable":false,"name":"NMR Spectroscopic Characterization of the C-Mannose Conformation in a Thrombospondin Repeat Using a Selective Labeling Approach.","description":"Despite the great interest in glycoproteins, structural information reporting on conformation and dynamics of the sugar moieties are limited. We present a new biochemical method to express proteins with glycans that are selectively labeled with NMR-active nuclei. We report on the incorporation of <sup>13</sup> C-labeled mannose in the C-mannosylated UNC-5 thrombospondin repeat. The conformational landscape of the C-mannose sugar puckers attached to tryptophan residues of UNC-5 is characterized by interconversion between the canonical <sup>1</sup> C<sub>4</sub> state and the B<sub>03</sub> / <sup>1</sup> S<sub>3</sub> state. This flexibility may be essential for protein folding and stabilization. We foresee that this versatile tool to produce proteins with selectively labeled C-mannose can ","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Nov","modification":"2026-05-03T00:13:45.125Z","creation":"2021-02-20T09:40:23Z"},"accession":"S-EPMC7692951","cross_references":{"pubmed":["32745319"],"doi":["10.1002/anie.202009489"]}}