biostudies-literatureJonker HRADeutsche ForschungsgemeinschaftHessisches Ministerium für Wissenschaft und Kunst20659-20665https://www.ebi.ac.uk/biostudies/studies/S-EPMC7692951biostudies-literatureUnknown59(46)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 Angewandte Chemie (International ed. in English)NMR Spectroscopic Characterization of the C-Mannose Conformation in a Thrombospondin Repeat Using a Selective Labeling Approach.PMC7692951FOR 2509BMRZJonker HRABakker HTiemann BSchwalbe HShcherbakova ASaxena KfalseNMR Spectroscopic Characterization of the C-Mannose Conformation in a Thrombospondin Repeat Using a Selective Labeling Approach.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 2020-01-01T00:00:00Z2020 Nov2026-05-03T00:13:45.125Z2021-02-20T09:40:23ZS-EPMC76929513274531910.1002/anie.202009489