ArticleBiophysical journal2002
Noncontact dipole effects on channel permeation. VI. 5F- and 6F-Trp gramicidin channel currents.
Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
11 citing papers in PubMed, 21 citations in OpenAlex.
- Molecular Mean-Field Theory of Ionic Solutions: A Poisson-Nernst-Planck-Bikerman Model.Entropy (Basel, Switzerland) · 2020Review
- Origin of the Shape of Current-Voltage Curve through Nanopores: A Molecular Dynamics Study.Scientific reports · 2016Article
- Quantum dynamics in continuum for proton transport--generalized correlation.The Journal of chemical physics · 2012Article
- Variational multiscale models for charge transport.SIAM review. Society for Industrial and Applied Mathematics · 2012Article
- The membrane interface dictates different anchor roles for "inner pair" and "outer pair" tryptophan indole rings in gramicidin A channels.Biochemistry · 2011Article
- Second-order Poisson Nernst-Planck solver for ion channel transport.Journal of computational physics · 2011Article
- The gramicidin channel ion permeation free-energy profile: direct and indirect effects of CHARMM force field improvements.Interdisciplinary sciences, computational life sciences · 2009Article
- The preference of tryptophan for membrane interfaces: insights from N-methylation of tryptophans in gramicidin channels.The Journal of biological chemistry · 2008Article
- Tryptophan contributions to the empirical free-energy profile in gramicidin A/M heterodimer channels.Biophysical journal · 2006Article
- Proton transfer in gramicidin water wires in phospholipid bilayers: attenuation by phosphoethanolamine.Biophysical journal · 2006Article
- Effects of phenylalanine substitutions in gramicidin A on the kinetics of channel formation in vesicles and channel structure in SDS micelles.Biophysical journal · 2005Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Fluorination of peptide side chains has been shown to perturb gramicidin channel conductance without significantly changing the average side chain structure, which, it is hoped, will allow detailed analysis of electrostatic modulation of current flow. Here we report a 1312-point potassium current-voltage-concentration data set for homodimeric channels formed from gramicidin A (gA) or any of eight fluorinated Trp analogs in both lecithin and monoglyceride bilayers. We fit the data with a three-barrier, two-site, two-ion (3B2S) kinetic model. The fluorination-induced changes in the rate constants were constrained by the same factor in both lipids. The rate constant changes were converted to transition-state free-energy differences for comparison with previous electrostatic potential energy differences based on an ab initio force field. The model allowed a reasonably good fit (chi = 8.29 with 1271 degrees of freedom). The measured changes were subtle. Nevertheless, the fitted energy perturbations agree well with electrostatic predictions for five of the eight peptides. For the other three analogs, the fitted changes suggested a reduced translocation barrier rather than the reduced exit barrier as predicted by electrostatics.
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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.