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Asymmetric maltose neopentyl glycol amphiphiles for a membrane protein study: effect of detergent asymmetricity on protein stability
Maintaining protein stability in an aqueous solution is a prerequisite for protein structural and functional studies, but conventional detergents have increasingly showed limited ability to maintain protein integrity. A representative novel agent, maltose neopentyl glycol-3 (MNG-3), has recently sub...
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| Vydáno v: | Chem Sci |
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| Hlavní autoři: | , , , , , , , , , , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
Royal Society of Chemistry
2018
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6346398/ https://ncbi.nlm.nih.gov/pubmed/30774908 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1039/c8sc02560f |
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