Entry STF0003
Horse apo-myoglobin
Protein information
| Name of the protein: | Myoglobin |
| Organism: | Equus caballus |
| Number of residues: | 153 |
| Related UniProt entry: | P68082 (Fragment: 2 - 154) |
| Related PDB entry: | 1YMB |
Visualize the data
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Experiment sets
EARLY
Method: Pulse labeling HDX MS
Conditions: pH 2.0-10.0; 0.0 Celsius; Probes: every amide site
Related publication:
PMID 20849085
Experiment details: "Protein refolding and pulsed HDX were carried out using a custom-made four-syringe continuous-flow setup with three sequential mixing steps. Syringe 1 was filled with an aqueous solution of 75 μM acid-unfolded aMb and 30 μM bradykinin in 10 mM HCl. Syringe 2 contained water with dilute ammonium hydroxide. Both syringes were connected to mixer M1 via fused silica capillaries. Refolding was initiated by mixing the contents of syringes 1 and 2 at M1 in a 1:1 volume ratio at a flow rate of 5 μl/min each, resulting in a pH jump from 2 to 10. The outlet of M1 was connected to a folding capillary. Depending on the folding time different capillary i.d. values and lengths were used (10 ms: i.d. 20 μm, l 5 mm; 100 ms: i.d. 50 μm, l 8.5 mm; 1 s: i.d. 75 μm, l 38 mm)."
Protection threshold: amide deuteration level <0.5 at 10ms of folding time
Sequence:
GLSDGEWQQVLNVWGKVEADIAGHGQEVLIRLFTGHPETLEKFDKFKHLKTEAEMKASEDLKKHGTVVLTALGGILKKKGHHEAELKPLAQSHATKHKIPIKYLEFISDAIIHVLHSKHPGDFGADAQGAMTKALELFRNDIAAKYKELGFQG
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EARLY residues
107: I;
108: S;
109: D;
110: A;
111: I;
112: I;
113: H;
114: V;
115: L;
116: H;
133: K;
134: A;
135: L;
136: E;
137: L;
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INTERMEDIATE
Method: Pulse labeling HDX MS
Conditions: pH 2.0-10.0; 0.0 Celsius; Probes: every amide site
Related publication:
PMID 20849085
Experiment details: "Protein refolding and pulsed HDX were carried out using a custom-made four-syringe continuous-flow setup with three sequential mixing steps. Syringe 1 was filled with an aqueous solution of 75 μM acid-unfolded aMb and 30 μM bradykinin in 10 mM HCl. Syringe 2 contained water with dilute ammonium hydroxide. Both syringes were connected to mixer M1 via fused silica capillaries. Refolding was initiated by mixing the contents of syringes 1 and 2 at M1 in a 1:1 volume ratio at a flow rate of 5 μl/min each, resulting in a pH jump from 2 to 10. The outlet of M1 was connected to a folding capillary. Depending on the folding time different capillary i.d. values and lengths were used (10 ms: i.d. 20 μm, l 5 mm; 100 ms: i.d. 50 μm, l 8.5 mm; 1 s: i.d. 75 μm, l 38 mm)."
Protection threshold: amide deuteration level 0.5-0.75 at 10ms of folding time
Sequence:
GLSDGEWQQVLNVWGKVEADIAGHGQEVLIRLFTGHPETLEKFDKFKHLKTEAEMKASEDLKKHGTVVLTALGGILKKKGHHEAELKPLAQSHATKHKIPIKYLEFISDAIIHVLHSKHPGDFGADAQGAMTKALELFRNDIAAKYKELGFQG
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INTERMEDIATE residues
138: F;
139: R;
142: I;
146: Y;
148: E;
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STRONG
Method: Native exchange MS
Conditions: pH 10.0; 0.0 Celsius; Probes: every amide site
Related publication:
PMID 20849085
Experiment details: "Protein refolding and pulsed HDX were carried out using a custom-made four-syringe continuous-flow setup with three sequential mixing steps. Syringe 1 was filled with an aqueous solution of 75 μM acid-unfolded aMb and 30 μM bradykinin in 10 mM HCl. Syringe 2 contained water with dilute ammonium hydroxide. Both syringes were connected to mixer M1 via fused silica capillaries. Refolding was initiated by mixing the contents of syringes 1 and 2 at M1 in a 1:1 volume ratio at a flow rate of 5 μl/min each, resulting in a pH jump from 2 to 10. The outlet of M1 was connected to a folding capillary. Depending on the folding time different capillary i.d. values and lengths were used (10 ms: i.d. 20 μm, l 5 mm; 100 ms: i.d. 50 μm, l 8.5 mm; 1 s: i.d. 75 μm, l 38 mm). Exchange was measured after one hour folding time."
Protection threshold: amide deuteration level < 0.25
Sequence:
GLSDGEWQQVLNVWGKVEADIAGHGQEVLIRLFTGHPETLEKFDKFKHLKTEAEMKASEDLKKHGTVVLTALGGILKKKGHHEAELKPLAQSHATKHKIPIKYLEFISDAIIHVLHSKHPGDFGADAQGAMTKALELFRNDIAAKYKELGFQG
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STRONG residues
8: Q;
9: Q;
10: V;
11: L;
12: N;
13: V;
14: W;
15: G;
16: K;
17: V;
18: E;
25: G;
26: Q;
27: E;
28: V;
29: L;
30: I;
31: R;
32: L;
33: F;
34: T;
35: G;
36: H;
40: L;
41: E;
45: K;
54: E;
55: M;
56: K;
67: V;
68: V;
69: L;
70: T;
128: Q;
129: G;
131: M;
133: K;
134: A;
135: L;
136: E;
137: L;
143: A;
146: Y;
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MEDIUM
Method: Native exchange MS
Conditions: pH 10.0; 0.0 Celsius; Probes: every amide site
Related publication:
PMID 20849085
Experiment details: "Protein refolding and pulsed HDX were carried out using a custom-made four-syringe continuous-flow setup with three sequential mixing steps. Syringe 1 was filled with an aqueous solution of 75 μM acid-unfolded aMb and 30 μM bradykinin in 10 mM HCl. Syringe 2 contained water with dilute ammonium hydroxide. Both syringes were connected to mixer M1 via fused silica capillaries. Refolding was initiated by mixing the contents of syringes 1 and 2 at M1 in a 1:1 volume ratio at a flow rate of 5 μl/min each, resulting in a pH jump from 2 to 10. The outlet of M1 was connected to a folding capillary. Depending on the folding time different capillary i.d. values and lengths were used (10 ms: i.d. 20 μm, l 5 mm; 100 ms: i.d. 50 μm, l 8.5 mm; 1 s: i.d. 75 μm, l 38 mm). Exchange was measured after one hour folding time."
Protection threshold: amide deuteration level 0.25-0.50
Sequence:
GLSDGEWQQVLNVWGKVEADIAGHGQEVLIRLFTGHPETLEKFDKFKHLKTEAEMKASEDLKKHGTVVLTALGGILKKKGHHEAELKPLAQSHATKHKIPIKYLEFISDAIIHVLHSKHPGDFGADAQGAMTKALELFRNDIAAKYKELGFQG
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MEDIUM residues
6: E;
7: W;
23: G;
24: H;
43: F;
44: D;
61: L;
62: K;
63: K;
106: F;
107: I;
108: S;
109: D;
110: A;
111: I;
112: I;
113: H;
114: V;
115: L;
116: H;
130: A;
132: T;
140: N;
142: I;
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WEAK
Method: Native exchange MS
Conditions: pH 10.0; 0.0 Celsius; Probes: every amide site
Related publication:
PMID 20849085
Experiment details: "Protein refolding and pulsed HDX were carried out using a custom-made four-syringe continuous-flow setup with three sequential mixing steps. Syringe 1 was filled with an aqueous solution of 75 μM acid-unfolded aMb and 30 μM bradykinin in 10 mM HCl. Syringe 2 contained water with dilute ammonium hydroxide. Both syringes were connected to mixer M1 via fused silica capillaries. Refolding was initiated by mixing the contents of syringes 1 and 2 at M1 in a 1:1 volume ratio at a flow rate of 5 μl/min each, resulting in a pH jump from 2 to 10. The outlet of M1 was connected to a folding capillary. Depending on the folding time different capillary i.d. values and lengths were used (10 ms: i.d. 20 μm, l 5 mm; 100 ms: i.d. 50 μm, l 8.5 mm; 1 s: i.d. 75 μm, l 38 mm). Exchange was measured after one hour folding time."
Protection threshold: amide deuteration level more than 0.50
Sequence:
GLSDGEWQQVLNVWGKVEADIAGHGQEVLIRLFTGHPETLEKFDKFKHLKTEAEMKASEDLKKHGTVVLTALGGILKKKGHHEAELKPLAQSHATKHKIPIKYLEFISDAIIHVLHSKHPGDFGADAQGAMTKALELFRNDIAAKYKELGFQG
CLICK TO DOWNLOAD SEQUENCE IN FASTA
WEAK residues
2: L;
3: S;
4: D;
5: G;
19: A;
20: D;
21: I;
22: A;
37: P;
38: E;
39: T;
42: K;
46: F;
47: K;
48: H;
49: L;
50: K;
51: T;
52: E;
53: A;
57: A;
58: S;
59: E;
60: D;
64: H;
65: G;
66: T;
71: A;
72: L;
73: G;
74: G;
75: I;
76: L;
77: K;
78: K;
79: K;
80: G;
81: H;
82: H;
83: E;
84: A;
85: E;
86: L;
87: K;
88: P;
89: L;
90: A;
91: Q;
92: S;
93: H;
94: A;
95: T;
96: K;
97: H;
98: K;
99: I;
100: P;
101: I;
102: K;
103: Y;
104: L;
105: E;
117: S;
118: K;
119: H;
120: P;
121: G;
122: D;
123: F;
124: G;
125: A;
126: D;
127: A;
138: F;
139: R;
141: D;
144: A;
145: K;
147: K;
148: E;
149: L;
150: G;
151: F;
152: Q;
153: G;
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