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Heat Modifiability of Outer Membrane Proteins from Gram-Negative Bacteria.

Authors :
Noinaj N
Kuszak AJ
Buchanan SK
Source :
Methods in molecular biology (Clifton, N.J.) [Methods Mol Biol] 2015; Vol. 1329, pp. 51-6.
Publication Year :
2015

Abstract

β-barrel membrane proteins are somewhat unique in that their folding states can be monitored using semi-native SDS-PAGE methods to determine if they are folded properly or not. This property, which is commonly referred to as heat modifiability, has been used for many years on both purified protein and on whole cells to monitor folded states of proteins of interest. Additionally, heat modifiability assays have proven indispensable in studying the BAM complex and its role in folding and inserting β-barrel membrane proteins into the outer membrane. Here, we describe the protocol our lab uses for performing the heat modifiability assay in our studies on outer membrane proteins.

Details

Language :
English
ISSN :
1940-6029
Volume :
1329
Database :
MEDLINE
Journal :
Methods in molecular biology (Clifton, N.J.)
Publication Type :
Academic Journal
Accession number :
26427675
Full Text :
https://doi.org/10.1007/978-1-4939-2871-2_4