{"title":"Solid-state NMR measurements of asymmetric dipolar couplings provide insight into protein side-chain motion","related_material":{"link":[{"relation":"erratum","url":"https://doi.org/10.1002/anie.201206663"}]},"quality_controlled":"1","extern":"1","date_published":"2011-09-14T00:00:00Z","citation":{"chicago":"Schanda, Paul, Matthias Huber, Jérôme Boisbouvier, Beat H. Meier, and Matthias Ernst. “Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion.” Angewandte Chemie International Edition. Wiley, 2011. https://doi.org/10.1002/anie.201103944.","apa":"Schanda, P., Huber, M., Boisbouvier, J., Meier, B. H., & Ernst, M. (2011). Solid-state NMR measurements of asymmetric dipolar couplings provide insight into protein side-chain motion. Angewandte Chemie International Edition. Wiley. https://doi.org/10.1002/anie.201103944","ista":"Schanda P, Huber M, Boisbouvier J, Meier BH, Ernst M. 2011. Solid-state NMR measurements of asymmetric dipolar couplings provide insight into protein side-chain motion. Angewandte Chemie International Edition. 50(46), 11005–11009.","mla":"Schanda, Paul, et al. “Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion.” Angewandte Chemie International Edition, vol. 50, no. 46, Wiley, 2011, pp. 11005–09, doi:10.1002/anie.201103944.","short":"P. Schanda, M. Huber, J. Boisbouvier, B.H. Meier, M. Ernst, Angewandte Chemie International Edition 50 (2011) 11005–11009.","ieee":"P. Schanda, M. Huber, J. Boisbouvier, B. H. Meier, and M. Ernst, “Solid-state NMR measurements of asymmetric dipolar couplings provide insight into protein side-chain motion,” Angewandte Chemie International Edition, vol. 50, no. 46. Wiley, pp. 11005–11009, 2011.","ama":"Schanda P, Huber M, Boisbouvier J, Meier BH, Ernst M. Solid-state NMR measurements of asymmetric dipolar couplings provide insight into protein side-chain motion. Angewandte Chemie International Edition. 2011;50(46):11005-11009. doi:10.1002/anie.201103944"},"intvolume":" 50","article_processing_charge":"No","year":"2011","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","month":"09","publication_identifier":{"issn":["1433-7851"]},"day":"14","publisher":"Wiley","author":[{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul","last_name":"Schanda","orcid":"0000-0002-9350-7606","first_name":"Paul"},{"full_name":"Huber, Matthias","first_name":"Matthias","last_name":"Huber"},{"full_name":"Boisbouvier, Jérôme","last_name":"Boisbouvier","first_name":"Jérôme"},{"last_name":"Meier","first_name":"Beat H.","full_name":"Meier, Beat H."},{"last_name":"Ernst","first_name":"Matthias","full_name":"Ernst, Matthias"}],"status":"public","date_created":"2020-09-18T10:09:40Z","abstract":[{"text":"Nonsymmetric motion: Solid‐state NMR measurements of dipolar coupling tensors provide insight into protein dynamics. The hitherto ignored asymmetry of the dipolar coupling tensor contains valuable information about motional asymmetry, which was used in the first direct site‐resolved measurement of such tensors. Important motions such as rotamer jumps can now be directly detected in the solid state.","lang":"eng"}],"volume":50,"date_updated":"2021-01-12T08:19:27Z","oa_version":"None","page":"11005-11009","article_type":"original","type":"journal_article","doi":"10.1002/anie.201103944","_id":"8464","publication":"Angewandte Chemie International Edition","language":[{"iso":"eng"}],"publication_status":"published","issue":"46"}