Start2Fold

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

Entry STF0039

Chymotrypsin Inhibitor 2

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Protein information

Name of the protein: Subtilisin-chymotrypsin inhibitor-2A
Organism: Hordeum vulgare (Barley)
Number of residues: 64
Related UniProt entry:   P01053 (Fragment: 19 - 84)
Related PDB entry:   3CI2

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Experiment sets

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STRONG

Method: Native exchange NMR

Conditions: pH 5.3; 33.0 Celsius; Probes: 34

Related publication:
 PMID 9231903

Experiment details: "Experiments were perfomed at 33 °C in 50 mM sodium acetate buffer (pH 5.3). The total salt concentration was maintained at 2.5 M throughout the range of GdmCl concentrations by addition of NaCl. Values of m and ΔGapp,0ex were calculated by fitting the exchange data at different [GdmCl] to the equation. Fitting was performed only when k(ex) could be measured for more than six [GdmCl]."

Protection threshold: ΔΔG(ex) = ΔΔG(global unfolding)

Sequence: HNLKTEWPELVGKSVEEAKKVILQDKPEAQIIVLPVGTIVTMEYRIDRVRLFVDKLDNIAQVPRVG
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STRONG residues

13: K; 22: I; 23: L; 32: I; 34: L; 49: V; 51: L; 52: F; 53: V;
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MEDIUM

Method: Native exchange NMR

Conditions: pH 5.3; 33.0 Celsius; Probes: 34

Related publication:
 PMID 9231903

Experiment details: "Experiments were perfomed at 33 °C in 50 mM sodium acetate buffer (pH 5.3). The total salt concentration was maintained at 2.5 M throughout the range of GdmCl concentrations by addition of NaCl. Values of m and ΔGapp,0ex were calculated by fitting the exchange data at different [GdmCl] to the equation. Fitting was performed only when k(ex) could be measured for more than six [GdmCl]."

Protection threshold: m > 2

Sequence: HNLKTEWPELVGKSVEEAKKVILQDKPEAQIIVLPVGTIVTMEYRIDRVRLFVDKLDNIAQVPRVG
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MEDIUM residues

7: W; 10: L; 11: V; 20: K; 21: V; 24: Q; 34: L; 48: R; 50: R; 54: D; 59: I; 60: A; 61: Q; 64: R;
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