Abstract:
:The temperature dependence of single-channel conductance and open probability for outer membrane protein A (OmpA) of Escherichia coli were examined in planar lipid bilayers. OmpA formed two interconvertible conductance states, small channels, 36-140 pS, between 15 and 37 degrees C, and large channels, 115-373 pS, between 21 and 39 degrees C. Increasing temperatures had strong effects on open probabilities and on the ratio of large to small channels, particularly between 22 and 34 degrees C, which effected sharp increases in average conductance. The data infer that OmpA is a flexible temperature-sensitive protein that exists as a small pore structure at lower temperatures, but refolds into a large pore at higher temperatures.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Zakharian E,Reusch RNdoi
10.1016/s0014-5793(03)01236-5keywords:
subject
Has Abstractpub_date
2003-12-04 00:00:00pages
229-35issue
2eissn
0014-5793issn
1873-3468pii
S0014579303012365journal_volume
555pub_type
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