Entry STF0012
French bean apoplastocyanin
Protein information
Name of the protein: | Plastocyanin |
Organism: | Phaseolus vulgaris |
Number of residues: | 99 |
Related UniProt entry: | P00287 (Fragment: 1 - 99) |
Related PDB entry: | 9PCY |
Visualize the data
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Experiment sets
EARLY
Method: HDX-folding competition by NMR
Conditions: pH 5.0-5.9; 25.0 Celsius; Probes: 29
Related publication:
PMID 8241116
Experiment details: "Apo-Pc was first exchanged by repetitive ultrafiltration into D2O buffer containing potassium phosphate (50 mM), NaCl (1 M), 2-mercaptoethanol (l0 mM), and EDTA (0.1 mM) (pH* 7.0, direct meter reading uncorrected for isotope effect). The protein was unfolded in the D2O buffer containing 2.2 M GuHCl and kept at 25C for 1 h. The refolding reaction was initiated by 1:21 dilution in D2O buffer without GuHCl. After a delay of 90 s to allow completion of the faster refolding reactions, the competition experiment was initiated by 1:9 dilution with either potassium phosphate (50 mM, pH 5.9) containing NaCl (1 M), 2-mercaptoethanol (10 mM), and EDTA (0.1 mM) in H2O or sodium acetate (50 mM, pH 5.0) containing NaCl (1.5 M), 2-mercaptoethanol (10 mM), and EDTA (0.1 mM) in H2O. The final pH values were 6.0 and 5.2, respectively."
Protection threshold: P > 20
Sequence:
LEVLLGSGDGSLVFVPSEFSVPSGEKIVFKNNAGFPHNVVFDEDEIPAGVDAVKISMPEEELLNAPGETYVVTLDTKGTYSFYCSPHQGAGMVGKVTVN
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EARLY residues
70: Y;
72: V;
80: Y;
82: F;
83: Y;
95: K;
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INTERMEDIATE
Method: HDX-folding competition by NMR
Conditions: pH 5.0-5.9; 25.0 Celsius; Probes: 29
Related publication:
PMID 8241116
Experiment details: "Apo-Pc was first exchanged by repetitive ultrafiltration into D2O buffer containing potassium phosphate (50 mM), NaCl (1 M), 2-mercaptoethanol (l0 mM), and EDTA (0.1 mM) (pH* 7.0, direct meter reading uncorrected for isotope effect). The protein was unfolded in the D2O buffer containing 2.2 M GuHCl and kept at 25C for 1 h. The refolding reaction was initiated by 1:21 dilution in D2O buffer without GuHCl. After a delay of 90 s to allow completion of the faster refolding reactions, the competition experiment was initiated by 1:9 dilution with either potassium phosphate (50 mM, pH 5.9) containing NaCl (1 M), 2-mercaptoethanol (10 mM), and EDTA (0.1 mM) in H2O or sodium acetate (50 mM, pH 5.0) containing NaCl (1.5 M), 2-mercaptoethanol (10 mM), and EDTA (0.1 mM) in H2O. The final pH values were 6.0 and 5.2, respectively."
Protection threshold: 10 < P < 20
Sequence:
LEVLLGSGDGSLVFVPSEFSVPSGEKIVFKNNAGFPHNVVFDEDEIPAGVDAVKISMPEEELLNAPGETYVVTLDTKGTYSFYCSPHQGAGMVGKVTVN
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INTERMEDIATE residues
4: L;
5: L;
15: V;
21: V;
27: I;
28: V;
98: V;
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LATE
Method: HDX-folding competition by NMR
Conditions: pH 5.0-5.9; 25.0 Celsius; Probes: 29
Related publication:
PMID 8241116
Experiment details: "Apo-Pc was first exchanged by repetitive ultrafiltration into D2O buffer containing potassium phosphate (50 mM), NaCl (1 M), 2-mercaptoethanol (l0 mM), and EDTA (0.1 mM) (pH* 7.0, direct meter reading uncorrected for isotope effect). The protein was unfolded in the D2O buffer containing 2.2 M GuHCl and kept at 25C for 1 h. The refolding reaction was initiated by 1:21 dilution in D2O buffer without GuHCl. After a delay of 90 s to allow completion of the faster refolding reactions, the competition experiment was initiated by 1:9 dilution with either potassium phosphate (50 mM, pH 5.9) containing NaCl (1 M), 2-mercaptoethanol (10 mM), and EDTA (0.1 mM) in H2O or sodium acetate (50 mM, pH 5.0) containing NaCl (1.5 M), 2-mercaptoethanol (10 mM), and EDTA (0.1 mM) in H2O. The final pH values were 6.0 and 5.2, respectively."
Protection threshold: 4 < P < 10
Sequence:
LEVLLGSGDGSLVFVPSEFSVPSGEKIVFKNNAGFPHNVVFDEDEIPAGVDAVKISMPEEELLNAPGETYVVTLDTKGTYSFYCSPHQGAGMVGKVTVN
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LATE residues
3: V;
40: V;
96: V;
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STRONG
Method: Native exchange NMR
Conditions: pH 7.0; 20.0 Celsius; Probes: all
Related publication:
PMID 3172230
Experiment details: "Very slowly exchanging amide protons were identified on the basis of observation of backbone NH/CH peaks in 2QF-COSY or 2Q spectra acquired 3.5 months after exchange into D2O at pH 7.0."
Protection threshold: very slowly exchanging amid protons
Sequence:
LEVLLGSGDGSLVFVPSEFSVPSGEKIVFKNNAGFPHNVVFDEDEIPAGVDAVKISMPEEELLNAPGETYVVTLDTKGTYSFYCSPHQGAGMVGKVTVN
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STRONG residues
3: V;
4: L;
5: L;
13: V;
14: F;
15: V;
21: V;
27: I;
28: V;
29: F;
30: K;
37: H;
38: N;
39: V;
40: V;
41: F;
70: Y;
72: V;
78: G;
80: Y;
82: F;
83: Y;
84: C;
94: G;
95: K;
96: V;
97: T;
98: V;
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