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Specific collapse followed by slow hydrogen-bond formation of β-sheet in the folding of single-chain monellin
Characterization of the conformational landscapes for proteins with different secondary structures is important in elucidating the mechanism of protein folding. The folding trajectory of single-chain monellin composed of a five-stranded β-sheet and a helix was investigated by using a pH-jump from th...
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| Hauptverfasser: | , , , , , , , |
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| Format: | Artigo |
| Sprache: | Inglês |
| Veröffentlicht: |
National Academy of Sciences
2005
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| Schlagworte: | |
| Online Zugang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC549438/ https://ncbi.nlm.nih.gov/pubmed/15710881 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0407982102 |
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