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Aromatic ring dynamics, thermal activation and transient conformations of a 468 kDa enzyme by specific (1)H-(13)C labeling and fast-MAS NMR
Aromatic residues are located at structurally important sites of many proteins. Probing their interactions and dynamics can provide important functional insight but is challenging in large proteins. Here, we introduce approaches to characterize dynamics of phenylalanine residues using (1)H-detected...
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| 出版年: | J Am Chem Soc |
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| 主要な著者: | , , , , , , , , , , , |
| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
2019
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| 主題: | |
| オンライン･アクセス: | https://ncbi.nlm.nih.gov/pmc/articles/PMC7302935/ https://ncbi.nlm.nih.gov/pubmed/31199882 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/jacs.9b04219 |
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