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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Gorde:
Xehetasun bibliografikoak
Argitaratua izan da:J Am Chem Soc
Egile Nagusiak: 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
Formatua: Artigo
Hizkuntza:Inglês
Argitaratua: 2019
Gaiak:
Article
Sarrera elektronikoa: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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