Mathew, MK and Balaram, P (1983) A helix dipole model for alamethicin and related transmembrane channels. In: FEBS Letters, 157 (1). pp. 1-5.
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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: | Journal Article |
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Publication: | FEBS Letters |
Publisher: | Elsevier |
Additional Information: | Copyright for this article belongs to Elsevier Science Ltd. |
Keywords: | membrane channel;alamethicin;helix dipole;amphipathic helix;membrane transport;peptide aggregation |
Department/Centre: | Division of Biological Sciences > Molecular Biophysics Unit |
Date Deposited: | 11 Mar 2005 |
Last Modified: | 19 Sep 2010 04:18 |
URI: | http://eprints.iisc.ac.in/id/eprint/2898 |
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