Monitoring ion channel conformations in membranes utilizing a novel dual fluorescence quenching approach

Kelkar, Devaki A. ; Chattopadhyay, Amitabha (2006) Monitoring ion channel conformations in membranes utilizing a novel dual fluorescence quenching approach Biochemical and Biophysical Research Communications, 343 (2). pp. 483-488. ISSN 0006-291X

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Official URL: http://linkinghub.elsevier.com/retrieve/pii/S00062...

Related URL: http://dx.doi.org/10.1016/j.bbrc.2006.02.163

Abstract

The linear peptide gramicidin forms prototypical ion channels specific for monovalent cations and has been extensively used to study the organization, dynamics, and function of membrane-spanning channels. We have analyzed the localization of the functionally important tryptophan residues of the membrane-bound channel and non-channel conformations of gramicidin utilizing a novel dual fluorescence quenching approach [G.A. Caputo, E. London, Biochemistry 42 (2003) 3265-3274]. In this paper, we show for the first time that the dual quenching approach is applicable to multiple tryptophan containing functional ion channel peptides such as gramicidin. Importantly, dual quenching is found to be sensitive to the membrane-bound conformations of this important model ion channel.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:Gramicidin; Ion Channel; Acrylamide Quenching; Dual Quenching; 10-DN; Non-channel
ID Code:7188
Deposited On:25 Oct 2010 12:19
Last Modified:16 May 2016 17:26

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