Protein conformational dynamics studied by (15)N and (1)H R(1ρ) relaxation dispersion: application to wild-type and G53A ubiquitin crystals

Solid-state NMR spectroscopy can provide site-resolved information about protein dynamics over many time scales. Here we combine protein deuteration, fast magic-angle spinning (~45 to 60 kHz) and proton detection to study dynamics of ubiquitin in microcrystals, and in particular a mutant in a region...

Täydet tiedot

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Bibliografiset tiedot
Julkaisussa:Solid State Nucl Magn Reson
Päätekijät: Gauto, Diego F., Hessel, Audrey, Rovó, Petra, Kurauskas, Vilius, Linser, Rasmus, Schanda, Paul
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: 2017
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Article
Linkit:https://ncbi.nlm.nih.gov/pmc/articles/PMC5531261/
https://ncbi.nlm.nih.gov/pubmed/28438365
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