Direct observation of fast protein folding: the initial collapse of apomyoglobin.
The rapid refolding dynamics of apomyoglobin are followed by a new temperature-jump fluorescence technique on a 15-ns to 0.5-ms time scale in vitro. The apparatus measures the protein-folding history in a single sweep in standard aqueous buffers. The earliest steps during folding to a compact state...
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| Publicado no: | Proc Natl Acad Sci U S A |
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| Principais autores: | , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
National Academy of Sciences
1996
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC39134/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8650166/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.93.12.5759 |
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