ArticleBiophysical journal2004
Monitoring gramicidin conformations in membranes: a fluorescence approach.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 76 citations in OpenAlex.
- Synthetic Lipid Biology.Chemical reviews · 2025Review
- Silica/Proteoliposomal Nanocomposite as a Potential Platform for Ion Channel Studies.Molecules (Basel, Switzerland) · 2022Article
- Measuring Membrane Penetration Depths and Conformational Changes in Membrane Peptides and Proteins.The Journal of membrane biology · 2022Review
- Monoclonal antibody stability can be usefully monitored using the excitation-energy-dependent fluorescence edge-shift.The Biochemical journal · 2020Article
- Activity and characterization of a pH-sensitive antimicrobial peptide.Biochimica et biophysica acta. Biomembranes · 2019Article
- Site-Directed Fluorescence Approaches for Dynamic Structural Biology of Membrane Peptides and Proteins.Frontiers in molecular biosciences · 2019Review
- Wavelength-Selective Fluorescence of a Model Transmembrane Peptide: Constrained Dynamics of Interfacial Tryptophan Anchors.Journal of fluorescence · 2018Article
- GFP fluorescence: A few lesser-known nuggets that make it work.Journal of biosciences · 2018Article
- Kinetics of peptide folding in lipid membranes.Biopolymers · 2015Review
- Organization and dynamics of tryptophan residues in brain spectrin: novel insight into conformational flexibility.Journal of fluorescence · 2015Article
- Importance of indole N-H hydrogen bonding in the organization and dynamics of gramicidin channels.Biochimica et biophysica acta · 2014Article
- pH dependent transfer of nano-pores into membrane of cancer cells to induce apoptosis.Scientific reports · 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
- A novel approach to the discovery of small-molecule ligands of CDK2.Chembiochem : a European journal of chemical biology · 2012Article
- Membrane organization and dynamics of "inner pair" and "outer pair" tryptophan residues in gramicidin channels.The journal of physical chemistry. B · 2012Article
- Exploring tryptophan dynamics in acid-induced molten globule state of bovine alpha-lactalbumin: a wavelength-selective fluorescence approach.European biophysics journal : EBJ · 2010Article
- Article
- Monitoring membrane protein conformational heterogeneity by fluorescence lifetime distribution analysis using the maximum entropy method.Journal of fluorescence · 2010Article
- Role of tryptophan residues in gramicidin channel organization and function.Biophysical journal · 2008Article
- Membrane interfacial localization of aromatic amino acids and membrane protein function.Journal of biosciences · 2006Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have monitored the membrane-bound channel and nonchannel conformations of gramicidin utilizing red-edge excitation shift (REES), and related fluorescence parameters. In particular, we have used fluorescence lifetime, polarization, quenching, chemical modification, and membrane penetration depth analysis in addition to REES measurements to distinguish these two conformations. Our results show that REES of gramicidin tryptophans can be effectively used to distinguish conformations of membrane-bound gramicidin. The interfacially localized tryptophans in the channel conformation display REES of 7 nm whereas the tryptophans in the nonchannel conformation exhibit REES of 2 nm which highlights the difference in their average environments in terms of localization in the membrane. This is supported by tryptophan penetration depth measurements using the parallax method and fluorescence lifetime and polarization measurements. Further differences in the average tryptophan microenvironments in the two conformations are brought out by fluorescence quenching experiments using acrylamide and chemical modification of the tryptophans by N-bromosuccinimide. In summary, we report novel fluorescence-based approaches to monitor conformations of this important ion channel peptide. Our results offer vital information on the organization and dynamics of the functionally important tryptophan residues in gramicidin.
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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.