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Unfolded states under folding conditions accommodate sequence-specific conformational preferences with random coil-like dimensions
Proteins are marginally stable molecules that fluctuate between folded and unfolded states. Here, we provide a high-resolution description of unfolded states under refolding conditions for the N-terminal domain of the L9 protein (NTL9). We use a combination of time-resolved Förster resonance energy...
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| Publicado no: | Proc Natl Acad Sci U S A |
|---|---|
| Main Authors: | , , , , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
National Academy of Sciences
2019
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC7056937/ https://ncbi.nlm.nih.gov/pubmed/31167941 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.1818206116 |
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