Start2Fold

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

Entry STF0017

Rabbit muscle aldolase

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Protein information

Name of the protein: Fructose-bisphosphate aldolase A
Organism: Oryctolagus cuniculus (Rabbit)
Number of residues: 363
Related UniProt entry:   P00883 (Fragment: 2 - 364)
Related PDB entry:   1ADO

Visualize the data

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Experiment sets

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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
 CLICK TO DOWNLOAD SEQUENCE IN FASTA

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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