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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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| Yayımlandı: | Biophys J |
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| Asıl Yazarlar: | , , , , , , |
| Materyal Türü: | Artigo |
| Dil: | Inglês |
| Baskı/Yayın Bilgisi: |
The Biophysical Society
2020
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| Konular: | |
| Online Erişim: | 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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