ArticleBiophysical journal2008
Role of tryptophan residues in gramicidin channel organization and function.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 40 citations in OpenAlex.
- Analyzing Transmembrane Protein and Hydrophobic Helix Topography by Dual Fluorescence Quenching.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Measuring Membrane Penetration Depths and Conformational Changes in Membrane Peptides and Proteins.The Journal of membrane biology · 2022Review
- Wavelength-Selective Fluorescence of a Model Transmembrane Peptide: Constrained Dynamics of Interfacial Tryptophan Anchors.Journal of fluorescence · 2018Article
- Characterizing Residue-Bilayer Interactions Using Gramicidin A as a Scaffold and Tryptophan Substitutions as Probes.Journal of chemical theory and computation · 2017Article
- Pore-forming Activity of the Escherichia coli Type III Secretion System Protein EspD.The Journal of biological chemistry · 2015Article
- Importance of indole N-H hydrogen bonding in the organization and dynamics of gramicidin channels.Biochimica et biophysica acta · 2014Article
- Membrane organization and dynamics of "inner pair" and "outer pair" tryptophan residues in gramicidin channels.The journal of physical chemistry. B · 2012Article
- Transmembrane helix dynamics of bacterial chemoreceptors supports a piston model of signalling.PLoS computational biology · 2011Article
- Exploring tryptophan dynamics in acid-induced molten globule state of bovine alpha-lactalbumin: a wavelength-selective fluorescence approach.European biophysics journal : EBJ · 2010Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The linear peptide gramicidin forms prototypical ion channels specific for monovalent cations and has been used extensively to study the organization, dynamics, and function of membrane-spanning channels. The tryptophan residues in gramicidin channels are crucial for maintaining the structure and function of the channel. We explored the structural basis for the reduction in channel conductance in the case of single-tryptophan analogs of gramicidin with three Trp --> hydrophobic substitutions using a combination of fluorescence approaches, which include red edge excitation shift and membrane penetration depth analysis, size-exclusion chromatography, and circular dichroism spectroscopy. We show here that the gramicidin analogs containing single-tryptophan residues adopt a mixture of nonchannel and channel conformations, as evident from analysis of membrane penetration depth, size-exclusion chromatography, and backbone circular dichroism data. These results are potentially useful in analyzing the effect of tryptophan substitution on the functioning of other ion channels and membrane proteins.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.