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Probing Membrane Topology of the Antimicrobial Peptide Distinctin by Solid-State NMR Spectroscopy in Zwitterionic and Charged Lipid Bilayers
Distinctin is a 47-residue antimicrobial peptide, which interacts with negatively charged membranes and is active against Gram-positive and Gram-negative bacteria. Its primary sequence comprises two linear chains of 22 (chain 1) and 25 (chain 2) residues, linked by a disulfide bridge between Cys19 o...
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| Asıl Yazarlar: | , , , , , , , , |
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| Materyal Türü: | Artigo |
| Dil: | Inglês |
| Baskı/Yayın Bilgisi: |
2010
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| Konular: | |
| Online Erişim: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2997851/ https://ncbi.nlm.nih.gov/pubmed/20719234 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.bbamem.2010.08.008 |
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