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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Detalhes bibliográficos
Publicado no:J Am Chem Soc
Main Authors: 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
Formato: Artigo
Idioma:Inglês
Publicado em: 2019
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Article
Acesso em linha: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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