ArticleThe journal of physical chemistry. B2012
Membrane organization and dynamics of "inner pair" and "outer pair" tryptophan residues in gramicidin channels.
Article in The journal of physical chemistry. B, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 19 citations in OpenAlex.
- Measuring Membrane Penetration Depths and Conformational Changes in Membrane Peptides and Proteins.The Journal of membrane biology · 2022Review
- Delving into Membrane Heterogeneity Utilizing Fluorescence Lifetime Distribution Analysis.The Journal of membrane biology · 2022Review
- Design, synthesis, and biological evaluation of stable βEuropean journal of medicinal chemistry · 2018Article
- Importance of indole N-H hydrogen bonding in the organization and dynamics of gramicidin channels.Biochimica et biophysica acta · 2014Article
- Interaction of a synthetic antimicrobial peptide with model membrane by fluorescence spectroscopy.European biophysics journal : EBJ · 2013Article
- Organization and dynamics of the N-terminal domain of chemokine receptor CXCR1 in reverse micelles: effect of graded hydration.The journal of physical chemistry. B · 2013Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
The linear ion channel peptide gramicidin serves as an excellent prototype for monitoring the organization, dynamics, and function of membrane-spanning channels. The tryptophan residues in gramicidin channels are crucial for establishing and maintaining the structure and function of the channel in the membrane bilayer. In order to address the basis of differential importance of tryptophan residues in the gramicidin channel, we monitored the effects of pairwise substitution of two of the four gramicidin tryptophans, the inner pair (Trp-9 and -11) and the outer pair (Trp-13 and -15), using a combination of steady state and time-resolved fluorescence approaches and circular dichroism spectroscopy. We show here that these double tryptophan gramicidin analogues adopt different conformations in membranes, suggesting that the conformational preference of double tryptophan gramicidin analogues is dictated by the positions of the tryptophans in the sequence. These results assume significance in the context of recent observations that the inner pair of tryptophans (Trp-9 and -11) is more important for gramicidin channel formation and channel conductance. These results could be potentially useful in analyzing the effect of tryptophan substitution on the functioning of ion channels and membrane proteins.
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Registered trials
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