NDLI: Monitoring Membrane Protein Conformational Heterogeneity by Fluorescence Lifetime Distribution Analysis Using the Maximum Entropy Method

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Monitoring Membrane Protein Conformational Heterogeneity by Fluorescence Lifetime Distribution Analysis Using the Maximum Entropy Method

Content Provider	Semantic Scholar
Author	Haldar, Sourav Kombrabail, Mamata Krishnamoorthy, Govindarajan Chattopadhyay, Amitabha
Copyright Year	2009
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.
Starting Page	407
Ending Page	413
Page Count	7
File Format	PDF HTM / HTML
DOI	10.1007/s10895-009-0554-z
Alternate Webpage(s)	http://repository.ias.ac.in/6986/1/352.pdf
PubMed reference number	19816758
Alternate Webpage(s)	https://doi.org/10.1007/s10895-009-0554-z
Journal	Medline
Volume Number	20
Journal	Journal of Fluorescence
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article

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