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Biological Magnetic Resonance Data BankA Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules |
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| Entry ID | Data summary | Entry Title | Citation Title | Authors |
|---|---|---|---|---|
| 19165 | 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 |