Structural heterogeneity in microcrystalline ubiquitin studied by solid-state NMR

By applying [1-(13)C]- and [2-(13)C]-glucose labeling schemes to the folded globular protein ubiquitin, a strong reduction of spectral crowding and increase in resolution in solid-state NMR (ssNMR) spectra could be achieved. This allowed spectral resonance assignment in a straightforward manner and...

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Detalhes bibliográficos
Publicado no:Protein Sci
Main Authors: Fasshuber, Hannes Klaus, Lakomek, Nils-Alexander, Habenstein, Birgit, Loquet, Antoine, Shi, Chaowei, Giller, Karin, Wolff, Sebastian, Becker, Stefan, Lange, Adam
Formato: Artigo
Idioma:Inglês
Publicado em: BlackWell Publishing Ltd 2015
Assuntos:
Accelerated Communications
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC4420510/
https://ncbi.nlm.nih.gov/pubmed/25644665
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/pro.2654
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