Mathew, M. K. ; Balaram, P. (1983) A helix dipole model for alamethicin and related transmembrane channels FEBS Letters, 157 (1). pp. 1-5. ISSN 0014-5793
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Official URL: http://linkinghub.elsevier.com/retrieve/pii/001457...
Related URL: http://dx.doi.org/10.1016/0014-5793(83)81105-3
Abstract
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.
| Item Type: | Article |
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| Source: | Copyright of this article belongs to Federation of European Biochemical Societies. |
| Keywords: | Membrane Channel; Alamethicin; Helix Dipole; Amphipathic Helix; Membrane Transport; Peptide Aggregation |
| ID Code: | 4200 |
| Deposited On: | 18 Oct 2010 09:12 |
| Last Modified: | 16 May 2016 14:53 |
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