Supplementary information
From the following article
Electrostatic couplings in OmpA ion-channel gating suggest a mechanism for pore opening
Heedeok Hong, Gabor Szabo & Lukas K Tamm
Nature Chemical Biology 2, 627 - 635 (2006) Published online: 15 October 2006
doi:10.1038/nchembio827
Supplementary Fig. 1
Unfolding transitions of wild-type and mutant OmpA in lipid bilayers measured by fluorescence spectroscopy.
Supplementary Fig. 2
Comparison of the SDS-PAGE patterns for the boiled samples of wild type, E52C R138C mutant, and the transmembrane domains of wild type and E52C R138C mutants in the presence and absence of 1%
ME.
Supplementary Fig. 3
SDS-PAGE of the outer-membrane fractions of E. coli BL21(DE3) mutant cells expressing wild-type and E52C R138C mutant OmpA with and without added 1% NaCl in the growth media.
Supplementary Fig. 4
Comparison of the growth behavior of E. coli BL21(DE3) mutant cells expressing the plasmid-coded OmpF in LB media with different NaCl concentrations.
Supplementary Fig. 5
Growth of E. coli BL21(DE3) mutant cells expressing the plasmid-coded E52C K82C mutant in the presence and absence of 0.05%
ME in LB media with no added NaCl.
Supplementary Fig. 6
Effects of sucrose on growth behavior of E. coli BL21(DE3) mutant cells expressing the plasmid-coded wild-type OmpA and E52C R138C mutant in the presence and absence of 0.05%
ME.
Supplementary Fig. 7
Additivity of m-value effects in double-mutant cycles for probing the interaction energies between the side chains in the gating region of the OmpA channel.
Supplementary Results
Analysis of additional double-mutant cycles and m values in double-mutant cycles.
Supplementary Methods
Supplementary biochemical, spectroscopic and analytical methods.
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