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The structure of a folding intermediate provides insight into differences in immunoglobulin amyloidogenicity
Folding intermediates play a key role in defining protein folding and assembly pathways as well as those of misfolding and aggregation. Yet, due to their transient nature, they are poorly accessible to high-resolution techniques. Here, we made use of the intrinsically slow folding reaction of an ant...
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| Hlavní autoři: | , , , , , , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
National Academy of Sciences
2008
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2533197/ https://ncbi.nlm.nih.gov/pubmed/18768806 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0802809105 |
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