期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 58, 期 17, 页码 5758-5762出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201811714
关键词
protein function; protein structure; proton detection; solid-state NMR spectroscopy; ultrafast MAS
资金
- Deutsche Forschungsgemeinschaft (Emmy Noether program) [SFB 749, TP A13, SFB 1309, TP 03]
- Verband der Chemischen Industrie (VCI, Liebig program)
- Excellence Cluster CiPS-M
- Excellence Cluster RESOLV
- Center for Nano-Science (CeNS)
Solid-state NMR spectroscopy has recently enabled structural biology with small amounts of non-deuterated proteins, largely alleviating the classical sample production demands. Still, despite the benefits for sample preparation, successful and comprehensive characterization of complex spin systems in the few cases of higher-molecular-weight proteins has thus far relied on traditional C-13-detected methodology or sample deuteration. Herein we show for a 29 kDa carbonic anhydrase: acetazolamide complex that different aspects of solid-state NMR assessment of a complex spin system can be successfully accessed using a non-deuterated, 500 mg sample in combination with adequate spectroscopic tools. The shown access to protein structure, protein dynamics, as well as biochemical parameters in amino acid sidechains, such as histidine protonation states, will be transferable to proteins that are not expressible in E. coli.
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