Start2Fold

The database of hydrogen/deuterium exchange data on protein folding and stability

Entry STF0041

Bacillus amyloliquefaciens ribonuclease

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Protein information

Name of the protein: Ribonuclease
Organism: Bacillus amyloliquefaciens (Bacillus velezensis)
Number of residues: 110
Related UniProt entry:   P00648 (Fragment: 48 - 157)
Related PDB entry:   1A2P

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Experiment sets

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STRONG

Method: Native exchange NMR

Conditions: pH 6.5-7.6; 33.0 Celsius; Probes: 41

Related publication:
 PMID 7626599

Experiment details: "20 mg of lyophilized l5N-labeled protein was in the appropriate buffer containing 90% H2O and 10% D2O. The exchange buffer was 20 mM deuterated imidazole, pD 6.7, or 50 mM deuterated Tris, pD 7.9, containing 0.05% sodium azide, dissolved in D2O. Approximately 20 mg of lyophilized, uniformly l5N-labeled protein was dissolved in the exchange buffer (final concentration ~3 mM), centrifuged, transferred to an NMR tube, and allowed to equilibrate in the magnet for 10 min before the start of the first NMR experiment. The first spectrum was recorded approximately 20 min after the solution of the protein. The sample was kept at 33 or 37 °C, in the NMR tubes, throughout the study, which lasted up to 3 months."

Protection threshold: k(obs) < E-05/min at pH 6.5 and k(obs) < 2E-04/min at pH 7.6

Sequence: AQVINTFDGVADYLQTYHKLPDNYITKSEAQALGWVASKGNLADVAPGKSIGGDIFSNREGKLPGKSGRTWREADINYTSGFRNSDRILYSSDWLIYKTTDHYQTFTKIR
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STRONG residues

14: L; 25: I; 74: A; 89: L; 97: Y;
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