Abstract: Chapter 7 Biological Solid-state NMR Spectroscopy Toshimichi Fujiwara, Toshimichi FujiwaraSearch for more papers by this author Toshimichi Fujiwara, Toshimichi FujiwaraSearch for more papers by this author Book Editor(s):Isao Suetake, Isao SuetakeSearch for more papers by this authorRohit K. Sharma, Rohit K. SharmaSearch for more papers by this authorHironobu Hojo, Hironobu HojoSearch for more papers by this author First published: 27 December 2022 https://doi.org/10.1002/9781119886358.ch7 AboutPDFPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShareShare a linkShare onEmailFacebookTwitterLinkedInRedditWechat Abstract Nuclear magnetic resonance (NMR) is a probe sensitive to the molecular structure and dynamics in solution and solid states. The difference in the molecular dynamics between solution and solid states leads to differences in experimental techniques and instrumentation in NMR. Zeeman interaction governs the resonance frequency of nuclear spin, which is proportional to the static magnetic field and is related to the NMR sensitivity. A sample with multiple conformations broadens the resonance lines due to the conformation-dependent isotropic chemical shifts. The structure of a membrane peptide tightly bound to phospholipid bilayer membranes has been determined by using internuclear distance and dihedral constraints obtained from Solid-state NMR. Molecular interactions in biological cells have been studied by solution NMR. Data analysis for such multidimensional NMR spectra has been a time-consuming step in the structural analysis, which requires considerable expertise. References Ernst , R.R. , Bodenhausen , G. , and Wokaun , A. ( 1987 ). Principles of Nuclear Magnetic Resonance in One and Two Dimensions . Oxford : Clarendon Press . Reif , B. , Ashbrook , S.E. , Emsley , L. , and Hong , M. ( 2021 ). Solid-state NMR spectroscopy . 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Publication Year: 2022
Publication Date: 2022-12-27
Language: en
Type: other
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