ArticleJournal of fluorescence2010
Monitoring membrane protein conformational heterogeneity by fluorescence lifetime distribution analysis using the maximum entropy method.
Article in Journal of fluorescence, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
7 citing papers in PubMed.
- Delving into Membrane Heterogeneity Utilizing Fluorescence Lifetime Distribution Analysis.The Journal of membrane biology · 2022Review
- Machine-learning model selection and parameter estimation from kinetic data of complex first-order reaction systems.PloS one · 2021Article
- Site-Directed Fluorescence Approaches for Dynamic Structural Biology of Membrane Peptides and Proteins.Frontiers in molecular biosciences · 2019Review
- Fluorescence spectroscopy for revealing mechanisms in biology: Strengths and pitfalls.Journal of biosciences · 2018Review
- Importance of indole N-H hydrogen bonding in the organization and dynamics of gramicidin channels.Biochimica et biophysica acta · 2014Article
- Analysis of simulated fluorescence intensities decays by a new maximum entropy method algorithm.Journal of fluorescence · 2013Article
- Membrane organization and dynamics of "inner pair" and "outer pair" tryptophan residues in gramicidin channels.The journal of physical chemistry. B · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Due to the inherent difficulty in crystallizing membrane proteins, approaches based on fluorescence spectroscopy have proved useful in elucidating their conformational characteristics. The ion channel peptide gramicidin serves as an excellent prototype for monitoring membrane protein conformation and dynamics due to a number of reasons. We have analyzed conformational heterogeneity in membrane-bound gramicidin using fluorescence lifetime distribution analysis of tryptophan residues by the maximum entropy method (MEM). MEM represents a model-free and robust approach for analyzing fluorescence lifetime distribution. In this paper, we show for the first time, that fluorescence lifetime distribution analysis using MEM could be a convenient approach to monitor conformational heterogeneity in membrane-bound gramicidin in particular and membrane proteins in general. Lifetime distribution analysis by MEM therefore provides a novel window to monitor conformational transitions in membrane proteins.
Indexed as
Identifiers
19816758What OpenQuestion holds
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.