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MPEx: a Tool for Exploring Membrane Proteins

Overview
Journal Protein Sci
Specialty Biochemistry
Date 2009 Sep 29
PMID 19785006
Citations 150
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Abstract

Hydropathy plot methods form a cornerstone of membrane protein research, especially in the early stages of biochemical and structural characterization. Membrane Protein Explorer (MPEx), described in this article, is a refined and versatile hydropathy-plot software tool for analyzing membrane protein sequences. MPEx is highly interactive and facilitates the characterization and identification of favorable protein transmembrane regions using experiment-based physical and biological hydrophobicity scales. Besides allowing the consequences of sequence mutations to be examined, it provides tools for aiding the design of membrane-active peptides. MPEx is freely available as a Java Web Start application from our web site at http://blanco.biomol.uci.edu/mpex.

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References
1.
Wimley W . Toward genomic identification of beta-barrel membrane proteins: composition and architecture of known structures. Protein Sci. 2002; 11(2):301-12. PMC: 2373429. DOI: 10.1110/ps.29402. View

2.
von Heijne G . Membrane protein structure prediction. Hydrophobicity analysis and the positive-inside rule. J Mol Biol. 1992; 225(2):487-94. DOI: 10.1016/0022-2836(92)90934-c. View

3.
Hristova K, White S . An experiment-based algorithm for predicting the partitioning of unfolded peptides into phosphatidylcholine bilayer interfaces. Biochemistry. 2005; 44(37):12614-9. DOI: 10.1021/bi051193b. View

4.
White S, Wimley W . Membrane protein folding and stability: physical principles. Annu Rev Biophys Biomol Struct. 1999; 28:319-65. DOI: 10.1146/annurev.biophys.28.1.319. View

5.
Fernandez-Vidal M, Jayasinghe S, Ladokhin A, White S . Folding amphipathic helices into membranes: amphiphilicity trumps hydrophobicity. J Mol Biol. 2007; 370(3):459-70. PMC: 2034331. DOI: 10.1016/j.jmb.2007.05.016. View