A helix dipole model for alamethicin and related transmembrane channels

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
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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