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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 |
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52200 | Chemical Shifts: 2 sets |
ModA - molybdate binding protein at two pHs (data with bound molybdate) |
Solution NMR chemical shift assignment of apo and molybdate-bound ModA at two pHs
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Hiep LD Nguyen, Karin A Crowhurst |
52193 | Chemical Shifts: 2 sets |
ModA - molybdate binding protein at two pHs |
Solution NMR chemical shift assignment of apo and molybdate-bound ModA at two pHs
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Hiep L Nguyen, Karin A Crowhurst |
50437 | Chemical Shifts: 2 sets |
Mutation that removes disulfide in HdeA results in an unfolded protein that gains structure at low pH |
Removal of disulfide from acid stress chaperone HdeA does not wholly eliminate structure or function at low pH
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Dane H Geddes-Buehre, Karin Crowhurst, M Imex Aguirre-Cardenas |
50421 | Chemical Shifts: 5 sets T1 Relaxation Values: 5 sets T2 Relaxation Values: 5 sets |
Detection of key sites of dimer dissociation and unfolding initiation during activation of acid-stress chaperone HdeA at low pH |
Detection of key sites of dimer dissociation and unfolding initiation during activation of acid-stress chaperone HdeA at low pH
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Jafaeth S Gomez, Jonathon M Benson, Karin A Crowhurst, Marlyn A Widjaja |
26638 | Chemical Shifts: 1 set |
Backbone and side chain chemical shift assignments of apolipophorin III from Galleria mellonella |
Backbone and side chain chemical shift assignments of apolipophorin III from Galleria mellonella
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James VC Horn, Karin A Crowhurst, Paul MM Weers |
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 |
15408 | Chemical Shifts: 1 set T1 Relaxation Values: 1 set T2 Relaxation Values: 1 set H Exchange Protection Factors: 1 set |
NMR-detected conformational exchange observed in a computationally designed variant of protein Gb1 |
NMR-detected conformational exchange observed in a computationally designed variant of protein Gb1
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Karin A Crowhurst, Stephen L Mayo |