Entry STF0046
Ribonuclease A
Protein information
Name of the protein: | Ribonuclease pancreatic |
Organism: | Bos taurus |
Number of residues: | 124 |
Related UniProt entry: | P61823 (Fragment: 27 - 150) |
Related PDB entry: | 1RBX |
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Experiment sets
STRONG
Method: Native exchange NMR
Conditions: pH 6.5; 35.0 Celsius; Probes: 46
Related publication:
PMID 7578123
Experiment details: "Prior to the HX reaction, RNase A was lyophilized from aqueous solution at pH 6.5 and sucrose was lyophilized twice from D2O solutions at pH* 6.5. HX reaction was initiated by dissolving the lyophilized protein into D2O. At different HX times, ranging from several minutes to about a week, aliquots (~0.6 mL) of the HX reaction were withdrawn and HX was quenched by dropping the pH* to 3.5 with DCl."
Protection threshold: strong protection
Sequence:
KETAAAKFERQHMDSSTSAASSSNYCNQMMKSRNLTKDRCKPVNTFVHESLADVQAVCSQKNVACKNGQTNCYQSYSTMSITDCRETGSSKYPNCAYKTTQANKHIIVACEGNPYVPVHFDASV
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STRONG residues
46: F;
47: V;
55: Q;
58: C;
73: Y;
74: Q;
79: M;
81: I;
106: I;
108: V;
109: A;
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EARLY
Method: Pulse labeling HDX NMR
Conditions: pH 4.0; 10.0 Celsius; Probes: 27
Related publication:
PMID 2236032
Experiment details: "The deuterated RNase A was unfolded in an unfolding buffer (2.65 M guanidine hydrochloride/40 mM glycine, in D2O at a final pH of 2). Refolding of the unfolded RNase A solution (60-70 mg of RNase A per ml) at pH 4 was initiated by diluting 10.5-fold into a refolding buffer (0.442 M sodium sulfate/0.055 M sodium formate, in H2O at pH 4.25). At different times after beginning refolding, the exchange pulse was initiated by diluting 1.5-fold into an exchange buffer [0.4 M sodium sulfate/0.25 M guanidine hydrochloride/0.1 M (final) glycine, in H2O] so that the final pH was 9 or 10. The 37-msec exchange pulse was terminated by diluting 1.33-fold into a quench buffer (0.4 M sodium sulfate/0.25 M guanidine hydrochloride/0.1 M sodium formate), so that the final pH was 2.9. The refolding reaction was then allowed to go to completion (10 min) at this pH. The mixing dead time was 5 msec for each of the three mixing events described above. For the zero time point, the exchange pulse was applied directly to the unfolded protein solution."
Protection threshold: strong protection in I1
Sequence:
KETAAAKFERQHMDSSTSAASSSNYCNQMMKSRNLTKDRCKPVNTFVHESLADVQAVCSQKNVACKNGQTNCYQSYSTMSITDCRETGSSKYPNCAYKTTQANKHIIVACEGNPYVPVHFDASV
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EARLY residues
47: V;
48: H;
54: V;
63: V;
72: C;
73: Y;
81: I;
84: C;
98: K;
106: I;
108: V;
116: V;
118: V;
119: H;
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INTERMEDIATE
Method: Pulse labeling HDX NMR
Conditions: pH 4.0; 10.0 Celsius; Probes: 27
Related publication:
PMID 2236032
Experiment details: "The deuterated RNase A was unfolded in an unfolding buffer (2.65 M guanidine hydrochloride/40 mM glycine, in D2O at a final pH of 2). Refolding of the unfolded RNase A solution (60-70 mg of RNase A per ml) at pH 4 was initiated by diluting 10.5-fold into a refolding buffer (0.442 M sodium sulfate/0.055 M sodium formate, in H2O at pH 4.25). At different times after beginning refolding, the exchange pulse was initiated by diluting 1.5-fold into an exchange buffer [0.4 M sodium sulfate/0.25 M guanidine hydrochloride/0.1 M (final) glycine, in H2O] so that the final pH was 9 or 10. The 37-msec exchange pulse was terminated by diluting 1.33-fold into a quench buffer (0.4 M sodium sulfate/0.25 M guanidine hydrochloride/0.1 M sodium formate), so that the final pH was 2.9. The refolding reaction was then allowed to go to completion (10 min) at this pH. The mixing dead time was 5 msec for each of the three mixing events described above. For the zero time point, the exchange pulse was applied directly to the unfolded protein solution."
Protection threshold: moderate protection in I1
Sequence:
KETAAAKFERQHMDSSTSAASSSNYCNQMMKSRNLTKDRCKPVNTFVHESLADVQAVCSQKNVACKNGQTNCYQSYSTMSITDCRETGSSKYPNCAYKTTQANKHIIVACEGNPYVPVHFDASV
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INTERMEDIATE residues
31: K;
34: N;
43: V;
59: S;
60: Q;
97: Y;
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