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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Publicat a:J Am Chem Soc
Autors principals: Gauto, Diego F., Macek, Pavel, Barducci, Alessandro, Fraga, Hugo, Hessel, Audrey, Terauchi, Tsutomu, Gajan, David, Miyanoiri, Yohei, Boisbouvier, Jerome, Lichtenecker, Roman, Kainosho, Masatsune, Schanda, Paul
Format: Artigo
Idioma:Inglês
Publicat: 2019
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Article
Accés en línia: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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