Entry ID | Original Release date | Data summary | Entry Title | Citation Title | Authors |
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19165 | 2013-12-12 | Chemical Shifts: 1 set |
Backbone and side chain chemical shift assignments of bacterial acid-stress chaperone HdeA at pH 6 |
NMR-monitored titration of acid-stress bacterial chaperone HdeA reveals that Asp and Glu charge neutralization produces a loosened dimer structure in preparation for protein unfolding and chaperone activation.
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Karin A Crowhurst, McKinzie A Garrison |