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Crystal structure of an amphiphilic foldamer reveals a 48-mer assembly comprising a hollow truncated octahedron
Foldamers provide an attractive medium to test the mechanisms by which biological macromolecules fold into complex three-dimensional structures, and ultimately to design novel protein-like architectures with properties unprecedented in nature. Here, we describe a large cage-like structure formed fro...
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| Main Authors: | , , , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
2014
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4013780/ https://ncbi.nlm.nih.gov/pubmed/24705140 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/ncomms4581 |
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