Start2Fold

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

Entry STF0032

Rabbit muscle triosephosphate isomerase

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Protein information

Name of the protein: Triosephosphate isomerase
Organism: Oryctolagus cuniculus (Rabbit)
Number of residues: 248
Related UniProt entry:   P00939 (Fragment: 1 - 248)
Related PDB entry:   1R2T

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Experiment sets

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EARLY

Method: Pulse labeling HDX MS

Conditions: pH 7.5; 22.0 Celsius; Probes: monitors MS segments almost covering the full protein

Related publication:
 PMID 15037083

Experiment details: "A stock solution of protein (60 mM in 5 mM phosphate buffer/ H2O (pH 7.5)) was diluted twofold with denaturing solution (6 M GdHCl/H2O, 5 mM phosphate, 1 mM DTT (pH 7.5)). After 24 hours incubation, the unfolded protein was diluted ten-fold with the renaturing buffer (5 mM phosphate/ H2O, 1 mM DTT (pH 7.5)) to initiate folding. After various folding times, the protein was labeled for three seconds by tenfold dilution with the labeling buffer (0.3 M GdDCl/D2O, 0.1 mM DTT (pH 7.5)) at 22 °C. The protein conc. during the folding step was about 3 mM. Isotope exchange was quenched by decreasing the pH to 2.5 and the temperature to 0.8 °C. The quench solution was 0.2 M HCl. Samples were stored at -80 °C until analyzed."

Protection threshold: fast folding domain

Sequence: APSRKFFVGGNWKMNGRKKNLGELITTLNAAKVPADTEVVCAPPTAYIDFARQKLDPKIAVAAQNCYKVTNGAFTGEISPGMIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALSEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWSKVVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPEFVDIINAKQ
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EARLY residues

109: I; 110: G; 111: Q; 112: K; 113: V; 114: A; 115: H; 116: A; 117: L; 118: S; 119: E; 120: G; 121: L; 122: G; 123: V; 124: I; 125: A; 126: C; 127: I; 128: G; 129: E; 130: K; 131: L; 132: D; 133: E; 134: R; 135: E; 136: A; 137: G; 138: I; 139: T; 140: E; 141: K; 142: V; 143: V; 144: F; 145: E; 146: Q; 147: T; 148: K; 149: V; 150: I; 151: A; 152: D; 153: N; 154: V; 155: K; 156: D; 157: W; 158: S; 159: K; 160: V; 161: V; 162: L; 163: A; 164: Y; 165: E; 166: P; 167: V; 168: W; 169: A; 170: I; 171: G; 172: T; 173: G; 174: K; 175: T; 176: A; 177: T; 178: P; 179: Q; 180: Q; 181: A; 182: Q; 183: E; 184: V; 185: H; 186: E; 187: K; 188: L; 189: R; 190: G; 191: W; 192: L; 193: K; 194: S; 195: N; 196: V; 197: S; 198: D; 199: A; 200: V; 201: A; 202: Q; 203: S; 204: T; 205: R; 206: I; 207: I; 208: Y; 209: G; 210: G; 211: S; 212: V; 213: T; 214: G; 215: A; 216: T; 217: C; 218: K; 219: E; 220: L; 221: A; 222: S; 223: Q; 224: P; 225: D; 226: V; 227: D; 228: G; 229: F; 230: L; 231: V; 232: G; 233: G; 234: A; 235: S; 236: L; 237: K; 238: P; 239: E; 240: F;
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LATE

Method: Pulse labeling HDX MS

Conditions: pH 7.5; 22.0 Celsius; Probes: monitors MS segments almost covering the full protein

Related publication:
 PMID 15037083

Experiment details: "A stock solution of protein (60 mM in 5 mM phosphate buffer/ H2O (pH 7.5)) was diluted twofold with denaturing solution (6 M GdHCl/H2O, 5 mM phosphate, 1 mM DTT (pH 7.5)). After 24 hours incubation, the unfolded protein was diluted ten-fold with the renaturing buffer (5 mM phosphate/ H2O, 1 mM DTT (pH 7.5)) to initiate folding. After various folding times, the protein was labeled for three seconds by tenfold dilution with the labeling buffer (0.3 M GdDCl/D2O, 0.1 mM DTT (pH 7.5)) at 22 °C. The protein conc. during the folding step was about 3 mM. Isotope exchange was quenched by decreasing the pH to 2.5 and the temperature to 0.8 °C. The quench solution was 0.2 M HCl. Samples were stored at -80 °C until analyzed."

Protection threshold: slow folding domain

Sequence: APSRKFFVGGNWKMNGRKKNLGELITTLNAAKVPADTEVVCAPPTAYIDFARQKLDPKIAVAAQNCYKVTNGAFTGEISPGMIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALSEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWSKVVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPEFVDIINAKQ
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LATE residues

1: A; 2: P; 3: S; 4: R; 5: K; 6: F; 7: F; 8: V; 9: G; 10: G; 11: N; 12: W; 13: K; 14: M; 15: N; 16: G; 17: R; 18: K; 19: K; 20: N; 21: L; 22: G; 23: E; 24: L; 25: I; 26: T; 27: T; 28: L; 29: N; 30: A; 31: A; 32: K; 33: V; 34: P; 35: A; 36: D; 37: T; 38: E; 39: V; 40: V; 41: C; 42: A; 43: P; 44: P; 45: T; 46: A; 47: Y; 48: I; 49: D; 50: F; 51: A; 52: R; 53: Q; 54: K; 55: L; 56: D; 57: P; 58: K; 59: I; 60: A; 61: V; 62: A; 63: A; 64: Q; 65: N; 66: C; 67: Y; 68: K; 69: V; 70: T; 71: N; 72: G; 73: A; 74: F; 75: T; 76: G; 77: E; 78: I; 79: S; 80: P; 81: G; 82: M; 83: I; 84: K; 85: D; 86: C; 87: G; 88: A; 89: T; 90: W; 91: V; 92: V; 93: L; 94: G; 95: H; 96: S; 97: E; 98: R; 99: R; 100: H; 101: V; 102: F; 103: G; 104: E; 105: S;
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