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Residual Structure of Unfolded Ubiquitin as Revealed by Hydrogen/Deuterium-Exchange 2D NMR

The characterization of residual structures persistent in unfolded proteins in concentrated denaturant solution is currently an important issue in studies of protein folding because the residual structure present, if any, in the unfolded state may form a folding initiation site and guide the subsequ...

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Bibliografiset tiedot
Julkaisussa:Biophys J
Päätekijät: Yagi-Utsumi, Maho, Chandak, Mahesh S., Yanaka, Saeko, Hiranyakorn, Methanee, Nakamura, Takashi, Kato, Koichi, Kuwajima, Kunihiro
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: The Biophysical Society 2020
Aiheet:
Linkit:https://ncbi.nlm.nih.gov/pmc/articles/PMC7732725/
https://ncbi.nlm.nih.gov/pubmed/33142107
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.bpj.2020.10.003
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