期刊论文详细信息
| FEBS Letters | |
| A helix dipole model for alamethicin and related transmembrane channels | |
| Mathew, M.K.1  Balaram, P.1  | |
| [1] Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India | |
| 关键词: Membrane channel; Alamethicin; Helix dipole; Amphipathic helix; Membrane transport; Peptide aggregation; | |
| DOI : 10.1016/0014-5793(83)81105-3 | |
| 学科分类:生物化学/生物物理 | |
| 来源: John Wiley & Sons Ltd. | |
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【 摘 要 】
A molecular model is proposed for the transmembrane channels formed by alamethicin and related polypeptides. The channels consist of an aggregate of rod-like helical polypeptides with a central aqueous core of ordered water. The helix dipole moment is considered to be the major factor modulating channel size, selectivity and field-dependent transitions.
【 授权许可】
Unknown
【 预 览 】
| Files | Size | Format | View |
|---|---|---|---|
| RO201912020284382ZK.pdf | 441KB |
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