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The crystal structure of a $3_{10}$ helical decapeptide containing \alpha-aminoisobutyric acid

Francis, AK and Iqbal, M and Balaram, P and Vijayan, M (1983) The crystal structure of a $3_{10}$ helical decapeptide containing \alpha-aminoisobutyric acid. In: FEBS Letters, 155 (2). pp. 230-232.


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Alamethicin and several related \alpha-aminoisobutyric acid (Aib) containing natural and synthetic peptides form voltage-dependent channels across lipid bilayer membranes [1,2]. Their high Aib content constrains these peptides to adopt $3_{10}$ [2,3] or \alpha-helical conformations [1,4]. Membrane channels are then formed by helical peptide aggregation in the lipid phase [l-35], with a major role for the macrodipole moment of the peptide helices in mediating monomer association and channel characteristics [2,6].

Item Type: Journal Article
Publication: FEBS Letters
Publisher: Elsevier
Additional Information: Copyright for this article belongs to Elsevier Science Ltd.
Keywords: channel forming ionophores;decapeptide;a-Aminoisobutyric acid;X-ray structure analysis;310 helix
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/2899

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