Entry STF0005
Bovine beta-lactoglobulin (beta-LG)
Protein information
| Name of the protein: | Beta-lactoglobulin |
| Organism: | Bos taurus |
| Number of residues: | 162 |
| Related UniProt entry: | P02754 (Fragment: 17 - 178) |
| Related PDB entry: | 3NPO |
Visualize the data
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Experiment sets
EARLY
Method: Pulse labeling HDX NMR
Conditions: pH 8.3; 6.0 Celsius; Probes: 80
Related publication:
PMID 10686102
Experiment details: "The H/2H exchange pulse labeling experiments were done manually at 6 C. The refolding of fully deuterated b-lactoglobulin was initiated from the TFE state in 40 % TFE (pH 3.0) or the Gdn-HCl-state in 6 MGdn-HCl (pH 3.0) by manually diluting 20-fold into D2O. At this stage, the pDr was confirmed to be 3.0. After the selected times (10, 30, 100 and 300 seconds) of refolding, the H/D exchange pulse labeling was carried out at pDr 8.3 by adding 1/100 volume of 250 mM Tris/D2O. For the refolding time zero at pDr 3.0, we directly diluted the denatured protein at pH 3.0 to the pulse labeling buffer at pDr 8.3. After an exchange pulse of 5 seconds at pDr 8.3, the reaction was quenched by lowering the pDr to 3.0. The denaturants and Tris were immediately removed by successive concentration/dilution of protein with 10 mM 2HCl. Throughout the procedures, the temperature of the solution was kept at 6 C. Then,HSQC spectra were measured to determine the extent of exchange at 25 C. The experiments were repeated twice and the results were similar within the error of +/-10%."
Protection threshold: proton occupancy > 0.7
Sequence:
LIVTQTMKGLDIQKVAGTWYSLAMAASDISLLDAQSAPLRVYVEELKPTPEGDLEILLQKWENDECAQKKIIAEKTKIPAVFKIDALNENKVLVLDTDYKKYLLFCMENSAEPEQSLVCQCLVRTPEVDDEALEKFDKALKALPMHIRLSFNPTQLEEQCHI
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EARLY residues
37: A;
54: L;
56: I;
57: L;
58: L;
61: W;
65: E;
92: V;
94: V;
102: Y;
103: L;
104: L;
105: F;
106: C;
107: M;
117: L;
118: V;
119: C;
120: Q;
122: L;
123: V;
127: E;
139: A;
140: L;
143: L;
145: M;
147: I;
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EARLY
Method: Burst phase labeling HDX NMR
Conditions: pH 7.0-10.7; 20.0 Celsius; Probes: 80
Related publication:
PMID 11175905
Experiment details: "Burst-phase labeling experiments at variable pulse pH and a constant refolding/exchange competition time of 1.8 ms"
Protection threshold: P > 10
Sequence:
LIVTQTMKGLDIQKVAGTWYSLAMAASDISLLDAQSAPLRVYVEELKPTPEGDLEILLQKWENGECAQKKIIAEKTKIPAVFKIDALNENKVLVLDTDYKKYLLFCMENSAEPEQSLACQCLVRTPEVDDEALEKFDKALKALPMHIRLSFNPTQLEEQCHI
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EARLY residues
93: L;
100: K;
106: C;
107: M;
117: L;
122: L;
123: V;
132: A;
133: L;
139: A;
141: K;
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INTERMEDIATE
Method: Burst phase labeling HDX NMR
Conditions: pH 7.0-10.7; 20.0 Celsius; Probes: 80
Related publication:
PMID 11175905
Experiment details: "Burst-phase labeling experiments at variable pulse pH and a constant refolding/exchange competition time of 1.8 ms"
Protection threshold: 5 < P < 10
Sequence:
LIVTQTMKGLDIQKVAGTWYSLAMAASDISLLDAQSAPLRVYVEELKPTPEGDLEILLQKWENGECAQKKIIAEKTKIPAVFKIDALNENKVLVLDTDYKKYLLFCMENSAEPEQSLACQCLVRTPEVDDEALEKFDKALKALPMHIRLSFNPTQLEEQCHI
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INTERMEDIATE residues
12: I;
21: S;
91: K;
118: A;
119: C;
120: Q;
129: D;
130: D;
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LATE
Method: Burst phase labeling HDX NMR
Conditions: pH 7.0-10.7; 20.0 Celsius; Probes: 80
Related publication:
PMID 11175905
Experiment details: "Burst-phase labeling experiments at variable pulse pH and a constant refolding/exchange competition time of 1.8 ms"
Protection threshold: 2 < P < 5
Sequence:
LIVTQTMKGLDIQKVAGTWYSLAMAASDISLLDAQSAPLRVYVEELKPTPEGDLEILLQKWENGECAQKKIIAEKTKIPAVFKIDALNENKVLVLDTDYKKYLLFCMENSAEPEQSLACQCLVRTPEVDDEALEKFDKALKALPMHIRLSFNPTQLEEQCHI
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LATE residues
14: K;
17: G;
18: T;
19: W;
90: N;
109: N;
116: S;
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STRONG
Method: Native exchange NMR
Conditions: pH 2.5; 45.0 Celsius; Probes: every amide site
Related publication:
PMID 10686102
Experiment details: "Corresponds to PDB code 3BLG! The H/D exchange was performed at 45 °C and pD 2.5 by dissolving the lyophilized protein into 10 mM DCl at a protein concentration of 10 mg/ml. The reaction was monitored by recording a series of 15N-1H HSQC spectra over four days."
Protection threshold: P > 10000
Sequence:
LIVTQTMKGLDIQKVAGTWYSLAMAASDISLLDAQSAPLRVYVEELKPTPEGDLEILLQKWENDECAQKKIIAEKTKIPAVFKIDALNENKVLVLDTDYKKYLLFCMENSAEPEQSLVCQCLVRTPEVDDEALEKFDKALKALPMHIRLSFNPTQLEEQCHI
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STRONG residues
15: V;
20: Y;
24: M;
54: L;
56: I;
59: Q;
91: K;
92: V;
93: L;
94: V;
95: L;
103: L;
104: L;
105: F;
106: C;
107: M;
108: E;
115: Q;
118: V;
119: C;
120: Q;
122: L;
123: V;
136: F;
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MEDIUM
Method: Native exchange NMR
Conditions: pH 2.5; 45.0 Celsius; Probes: every amide site
Related publication:
PMID 10686102
Experiment details: "Corresponds to PDB code 3BLG! The H/D exchange was performed at 45 °C and pD 2.5 by dissolving the lyophilized protein into 10 mM DCl at a protein concentration of 10 mg/ml. The reaction was monitored by recording a series of 15N-1H HSQC spectra over four days."
Protection threshold: 5000 < P < 10000
Sequence:
LIVTQTMKGLDIQKVAGTWYSLAMAASDISLLDAQSAPLRVYVEELKPTPEGDLEILLQKWENDECAQKKIIAEKTKIPAVFKIDALNENKVLVLDTDYKKYLLFCMENSAEPEQSLVCQCLVRTPEVDDEALEKFDKALKALPMHIRLSFNPTQLEEQCHI
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MEDIUM residues
19: W;
23: A;
25: A;
43: V;
67: A;
84: I;
121: C;
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WEAK
Method: Native exchange NMR
Conditions: pH 2.5; 45.0 Celsius; Probes: every amide site
Related publication:
PMID 10686102
Experiment details: "Corresponds to PDB code 3BLG! The H/D exchange was performed at 45 °C and pD 2.5 by dissolving the lyophilized protein into 10 mM DCl at a protein concentration of 10 mg/ml. The reaction was monitored by recording a series of 15N-1H HSQC spectra over four days."
Protection threshold: 1000 < P < 5000
Sequence:
LIVTQTMKGLDIQKVAGTWYSLAMAASDISLLDAQSAPLRVYVEELKPTPEGDLEILLQKWENDECAQKKIIAEKTKIPAVFKIDALNENKVLVLDTDYKKYLLFCMENSAEPEQSLVCQCLVRTPEVDDEALEKFDKALKALPMHIRLSFNPTQLEEQCHI
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WEAK residues
16: A;
32: L;
41: V;
46: L;
57: L;
58: L;
71: I;
73: A;
74: E;
81: V;
82: F;
90: N;
102: Y;
109: N;
139: A;
140: L;
143: L;
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