A fast MAS 1H NMR study of amino acids and proteins |
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| Institution: | 1. Department of Chemistry, University of Aveiro, 3810-193 Aveiro, Portugal;2. Ruder Boškovic Institute, P.O. Box 180, 10002 Zagreb, Croatia;1. State Key Laboratory of Green Building Materials, China Building Materials Academy, 100024 Beijing, China;2. NeoTrident Technology Ltd., 201204 Shanghai, China;3. Department of Chemistry, Shandong University, 250100 Jinan, China;1. School of Advanced Materials Science and Engineering, Kumoh National Institute of Technology, Gumi, Gyeongbuk 730-701, Republic of Korea;2. Department of Materials Science and Engineering and RIAM, Seoul National University, Seoul 151-744, Republic of Korea;1. Shanghai Key Laboratory of Magnetic Resonance, School of Physics and Materials Science, East China Normal University, Shanghai 200062, PR China;2. Bruker BioSpin GmbH, 4 Silberstreifen, 76287 Rheinstetten, Germany;3. Univ. Lille, UMR 8181, UCCS: Unit of Catalysis and Chemistry of Solids, 59000 Lille, France;4. Bruker France, 34 Rue de l’Industrie, 67166 Wissembourg, France;5. Institut Universitaire de France, 1 Rue Descartes, 75231 Paris, France;1. Materials Science and Engineering Department, University of Wisconsin-Milwaukee, Milwaukee, WI 53211, USA;2. Materials Science and Engineering Department, Yonsei University, Seoul 120-749, South Korea;3. Computer Engineering Department, Hongik University, Seoul 121-791, South Korea;4. U.S. Army Research Laboratory, Weapons and Materials Research Directorate, Aberdeen Proving Ground, MD 21005, USA |
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| Abstract: | Fast sample spinning (up to 32 kHz) in tandem with delayed acquisition enabled resolved 1H NMR spectra of solid amino acids to be recorded. The resulting spectra are, however, significantly dependent on sample crystallinity and on sample preparation conditions, e.g. sample drying. Sample heating leads to a marked increase in signal to noise ratio and enables groups with different dynamic properties to be identified. In addition, the observation of peak shifts as a function of heating allows the identification of hydrogen bonded sites. Spectral assignment of the 1H MAS spectra is proposed for some examples based on relaxation properties, study of deuteriated samples and 2D NMR. The effects of molecular weight and sample complexity on the 1H MAS spectra were investigated using tetraglycine, polyglycine and two proteins: a small protein (lysozyme) and a much larger protein (a cereal storage protein named high molecular weight subunit 1Dx5). Moderate spectral resolution was achieved for the peptides and lysozyme, but for 1Dx5, significant resolution enhancement was obtained enabling the identification of resonances in all regions of the spectra including the alpha region, the aromatic region and the NH backbone region. |
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