A helix dipole model for alamethicin and related transmembrane channels

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
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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