Entry STF0032
Rabbit muscle triosephosphate isomerase
Protein information
| Name of the protein: | Triosephosphate isomerase |
| Organism: | Oryctolagus cuniculus |
| Number of residues: | 248 |
| Related UniProt entry: | P00939 (Fragment: 1 - 248) |
| Related PDB entry: | 1R2T |
Visualize the data
Click here or on the image on the right to visualize the residues using JSmol. Warning: JSmol is known to load slowly on certain browsers, depending on the size of the macromolecule. The applet is optimized for Chrome, other browsers have limited support.
Experiment sets
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
CLICK TO DOWNLOAD SEQUENCE IN FASTA
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;
CLICK TO DOWNLOAD LIST OF RESIDUES
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
CLICK TO DOWNLOAD SEQUENCE IN FASTA
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;
CLICK TO DOWNLOAD LIST OF RESIDUES