{"issue":"49","doi":"10.1002/anie.200904411","_id":"8474","article_processing_charge":"No","type":"journal_article","page":"9322-9325","volume":48,"day":"17","citation":{"short":"P. Schanda, M. Huber, R. Verel, M. Ernst, B. Meier, Angewandte Chemie International Edition 48 (2009) 9322–9325.","apa":"Schanda, P., Huber, M., Verel, R., Ernst, M., &#38; Meier, B. (2009). Direct detection of 3hJN’ hydrogen-bond scalar couplings in proteins by solid-state NMR spectroscopy. <i>Angewandte Chemie International Edition</i>. Wiley. <a href=\"https://doi.org/10.1002/anie.200904411\">https://doi.org/10.1002/anie.200904411</a>","ieee":"P. Schanda, M. Huber, R. Verel, M. Ernst, and B. Meier, “Direct detection of 3hJN’ hydrogen-bond scalar couplings in proteins by solid-state NMR spectroscopy,” <i>Angewandte Chemie International Edition</i>, vol. 48, no. 49. Wiley, pp. 9322–9325, 2009.","ama":"Schanda P, Huber M, Verel R, Ernst M, Meier B. Direct detection of 3hJN’ hydrogen-bond scalar couplings in proteins by solid-state NMR spectroscopy. <i>Angewandte Chemie International Edition</i>. 2009;48(49):9322-9325. doi:<a href=\"https://doi.org/10.1002/anie.200904411\">10.1002/anie.200904411</a>","ista":"Schanda P, Huber M, Verel R, Ernst M, Meier B. 2009. Direct detection of 3hJN’ hydrogen-bond scalar couplings in proteins by solid-state NMR spectroscopy. Angewandte Chemie International Edition. 48(49), 9322–9325.","mla":"Schanda, Paul, et al. “Direct Detection of 3hJN’ Hydrogen-Bond Scalar Couplings in Proteins by Solid-State NMR Spectroscopy.” <i>Angewandte Chemie International Edition</i>, vol. 48, no. 49, Wiley, 2009, pp. 9322–25, doi:<a href=\"https://doi.org/10.1002/anie.200904411\">10.1002/anie.200904411</a>.","chicago":"Schanda, Paul, Matthias Huber, René Verel, Matthias Ernst, and Beat H. Meier. “Direct Detection of 3hJN’ Hydrogen-Bond Scalar Couplings in Proteins by Solid-State NMR Spectroscopy.” <i>Angewandte Chemie International Edition</i>. Wiley, 2009. <a href=\"https://doi.org/10.1002/anie.200904411\">https://doi.org/10.1002/anie.200904411</a>."},"abstract":[{"lang":"eng","text":"Hydrogen bonds are ubiquitous interactions in proteins, and are important for their folding and functionality. Scalar coupling constants across hydrogen bonds in the protein backbone, some as small as 0.5 Hz, can be directly measured in the solid state by NMR spectroscopy (see figure). The nuclei on both sides of the hydrogen bond can be identified and the size of the coupling constant can be measured accurately."}],"author":[{"last_name":"Schanda","first_name":"Paul","orcid":"0000-0002-9350-7606","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul"},{"full_name":"Huber, Matthias","last_name":"Huber","first_name":"Matthias"},{"full_name":"Verel, René","first_name":"René","last_name":"Verel"},{"full_name":"Ernst, Matthias","first_name":"Matthias","last_name":"Ernst"},{"last_name":"Meier","first_name":"Beat H.","full_name":"Meier, Beat H."}],"title":"Direct detection of 3hJN' hydrogen-bond scalar couplings in proteins by solid-state NMR spectroscopy","date_published":"2009-11-17T00:00:00Z","quality_controlled":"1","oa_version":"None","year":"2009","language":[{"iso":"eng"}],"extern":"1","month":"11","publication_identifier":{"issn":["1433-7851","1521-3773"]},"keyword":["General Chemistry","Catalysis"],"publication":"Angewandte Chemie International Edition","publication_status":"published","article_type":"original","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","status":"public","intvolume":"        48","date_updated":"2021-01-12T08:19:31Z","date_created":"2020-09-18T10:11:33Z","publisher":"Wiley"}