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Comparisons of Interfacial Phe, Tyr, and Trp Residues as Determinants of Orientation and Dynamics for GWALP Transmembrane Peptides
[Image: see text] Aromatic amino acids often flank the transmembrane alpha helices of integral membrane proteins. By favoring locations within the membrane–water interface of the lipid bilayer, aromatic residues Trp, Tyr, and sometimes Phe may serve as anchors to help stabilize a transmembrane orien...
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| 主要な著者: | , , , , , |
|---|---|
| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
American
Chemical Society
2014
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| オンライン・アクセス: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4053069/ https://ncbi.nlm.nih.gov/pubmed/24829070 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi500439x |
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