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Characterization of a 22-residue peptide derived from a designed ion channel

Seth, S and Balaram, P and Mathew, MK (1997) Characterization of a 22-residue peptide derived from a designed ion channel. In: Biochimica Et Biophysica Acta-Biomembranes, 1328 (2). pp. 177-184.

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We have designed a four-helix protein that is expected to tetramerize in the membrane to form an ion channel with a structurally well-defined pore. This should serve as a model system to study the structural requirements of voltage-sensitive, ion-selective transmembrane channels. We have synthesized the peptide corresponding to the channel-lining helix. Circular dichroism (CD) spectroscopy shows that this peptide is helical in the membrane. Fluorescence resonance energy transfer (FRET) shows that this peptide, at low concentrations, forms aggregates in 1,2-dimyristoyl-sn-glycero-3-phosphatidylcholine (DMPC) liposomes and facilitates ion transport across liposomal membranes. Our data indicate that a component of the designed four-helix protein, i.e., the channel-lining helix, behaves as per design.

Item Type: Journal Article
Publication: Biochimica Et Biophysica Acta-Biomembranes
Publisher: Elsevier Science
Additional Information: Copyright of this article belongs to Elsevier Science.
Keywords: Protein design;peptide synthesis;ion transport; iposome;circular dichroism;fluorescence resonance energy transfer.
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 29 May 2009 06:46
Last Modified: 19 Sep 2010 05:24
URI: http://eprints.iisc.ac.in/id/eprint/18667

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