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Negatively charged amino acid residues play an active role in orienting the Sec-independent Pf3 coat protein in the Escherichia coli inner membrane.
The coat protein of Pseudomonas aeruginosa phage Pf3 is transiently inserted into the bacterial inner membrane with a single transmembrane anchor sequence in the N(out)C(in) orientation. The N-terminal sequence immediately flanking the membrane anchor contains one negatively charged residue, whereas...
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| 主要な著者: | , , , |
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| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
1997
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| 主題: | |
| オンライン・アクセス: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1169822/ https://ncbi.nlm.nih.gov/pubmed/9171335 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/emboj/16.9.2197 |
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