Entry STF0017
Rabbit muscle aldolase
Protein information
| Name of the protein: | Fructose-bisphosphate aldolase A |
| Organism: | Oryctolagus cuniculus |
| Number of residues: | 363 |
| Related UniProt entry: | P00883 (Fragment: 2 - 364) |
| Related PDB entry: | 1ADO |
Visualize the data
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Experiment sets
EARLY
Method: Pulse labeling HDX MS
Conditions: pH 7.0; 37.0 Celsius; Probes: >30
Related publication:
PMID 12741828
Experiment details: "Unfolded in 6 M GdHCl [H2O, 50 mM phosphate buffer (pH 7.0), 10 mM DTT, and 1 mM EDTA] for 24 h. Folding was initiated by decreasing the concentration of GdHCl through dialysis into a solution of the same composition, but with no GdHCl."
Protection threshold: residues of first protected segments
Sequence:
PHSHPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKYSHEEIAMATVTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRALANSLACQGKYTSSGQAGAAASESLFISNHAY
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EARLY residues
1: P;
2: H;
3: S;
4: H;
5: P;
6: A;
7: L;
8: T;
9: P;
10: E;
11: Q;
12: K;
13: K;
14: E;
15: L;
16: S;
17: D;
144: F;
145: A;
146: K;
147: W;
148: R;
149: C;
150: V;
151: L;
163: I;
164: M;
165: E;
166: N;
167: A;
168: N;
169: V;
170: L;
204: V;
205: T;
206: E;
207: K;
208: V;
209: L;
210: A;
211: A;
255: A;
256: L;
257: R;
258: R;
259: T;
260: V;
261: P;
262: P;
263: A;
264: V;
265: T;
266: G;
267: V;
268: T;
269: F;
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INTERMEDIATE
Method: Pulse labeling HDX MS
Conditions: pH 7.0; 37.0 Celsius; Probes: >30
Related publication:
PMID 12741828
Experiment details: "Unfolded in 6 M GdHCl [H2O, 50 mM phosphate buffer (pH 7.0), 10 mM DTT, and 1 mM EDTA] for 24 h. Folding was initiated by decreasing the concentration of GdHCl through dialysis into a solution of the same composition, but with no GdHCl."
Protection threshold: residues of intermediately protected segments
Sequence:
PHSHPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKYSHEEIAMATVTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRALANSLACQGKYTSSGQAGAAASESLFISNHAY
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INTERMEDIATE residues
31: A;
32: A;
33: D;
34: E;
35: S;
36: T;
37: G;
38: S;
39: I;
40: A;
41: K;
42: R;
43: L;
44: Q;
45: S;
46: I;
47: G;
48: T;
49: E;
50: N;
51: T;
52: E;
53: E;
171: A;
172: R;
173: Y;
174: A;
175: S;
176: I;
177: C;
178: Q;
179: Q;
180: N;
181: G;
182: I;
183: V;
184: P;
185: I;
186: V;
187: E;
229: K;
230: P;
231: N;
232: M;
233: V;
234: T;
235: P;
236: G;
237: H;
238: A;
284: N;
285: A;
286: I;
287: N;
288: K;
289: C;
290: P;
291: L;
292: L;
293: K;
294: P;
295: W;
296: A;
297: L;
298: T;
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STRONG
Method: Native exchange MS
Conditions: pH 6.8; 25.0 Celsius; Probes: >30
Related publication:
PMID 9572840
Experiment details: "Rabbit muscle aldolase was equilibrated in 5 mM phosphate/H2O buffer (pH 6.8, 25°C) for approximately 1 h, then transferred to a urea/H2O solution (3 M urea, 5 mM phosphate, pH 6.8, 25°C), where it was incubated for 3 min to 48 h. The aldolase concentration in this solution was 0.2 mM. Unfolded regions of aldolase were labeled by diluting the solution 20-fold with urea/D2O buffer (3 M urea, 5 mM phosphate, pH 6.8, 25°C). Isotopic exchange was quenched after 10 s by decreasing the pH and temperature (pH 2.5, 0°C)."
Protection threshold: very slow exchange
Sequence:
PHSHPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKYSHEEIAMATVTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRALANSLACQGKYTSSGQAGAAASESLFISNHAY
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STRONG residues
166: N;
167: A;
168: N;
169: V;
170: L;
203: Y;
204: V;
205: T;
206: E;
251: A;
252: T;
253: V;
254: T;
255: A;
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MEDIUM
Method: Native exchange MS
Conditions: pH 6.8; 25.0 Celsius; Probes: >30
Related publication:
PMID 9572840
Experiment details: "Rabbit muscle aldolase was equilibrated in 5 mM phosphate/H2O buffer (pH 6.8, 25°C) for approximately 1 h, then transferred to a urea/H2O solution (3 M urea, 5 mM phosphate, pH 6.8, 25°C), where it was incubated for 3 min to 48 h. The aldolase concentration in this solution was 0.2 mM. Unfolded regions of aldolase were labeled by diluting the solution 20-fold with urea/D2O buffer (3 M urea, 5 mM phosphate, pH 6.8, 25°C). Isotopic exchange was quenched after 10 s by decreasing the pH and temperature (pH 2.5, 0°C)."
Protection threshold: slow exchange (rate constants ~0.0064 ± 0.0010 s(-1))
Sequence:
PHSHPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKYSHEEIAMATVTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRALANSLACQGKYTSSGQAGAAASESLFISNHAY
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MEDIUM residues
1: P;
2: H;
3: S;
4: H;
5: P;
6: A;
7: L;
8: T;
9: P;
10: E;
11: Q;
12: K;
13: K;
14: E;
15: L;
16: S;
17: D;
152: K;
153: I;
154: G;
155: E;
156: H;
157: T;
158: P;
159: S;
160: A;
161: L;
162: A;
171: A;
172: R;
173: Y;
174: A;
175: S;
176: I;
177: C;
178: Q;
179: Q;
180: N;
181: G;
182: I;
183: V;
184: P;
185: I;
186: V;
187: E;
255: A;
256: L;
257: R;
258: R;
259: T;
260: V;
261: P;
262: P;
263: A;
264: V;
265: T;
266: G;
267: V;
268: T;
269: F;
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