Start2Fold

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

Entry STF0047

Tendamistat

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Protein information

Name of the protein: Alpha-amylase inhibitor HOE-467A
Organism: Streptomyces tendae
Number of residues: 74
Related UniProt entry:   P01092 (Fragment: 31 - 104)
Related PDB entry:   1OK0

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Experiment sets

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STRONG

Method: Native exchange NMR

Conditions: pH 3.0; 50.0 Celsius; Probes: 50

Related publication:
 PMID 2827730

Experiment details: "A sample of the dry protein was first mixed with D2O. The resulting pD value to the isoelectric for Tendamistat, and the protein remained undissolved. The D2O was removed once by lyophilization. Then a 3 mM solution of the protein in 99.8% D2O was prepared by titrating the pD to 3.0 with a deuteriated perchloric acid solution. Eight NMR samples were removed from the stock solution and heated to 50 °C for 0, 5, 20, 100, 240, 480, 1020, and 4200 min, respectively."

Protection threshold: P > 3000

Sequence: DTTVSEPAPSCVTLYQSWRYSQADNGCAETVTVKVVYEDDTEGLCYAVAPGQITTVGDGYIGSHGHARYLARCL
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STRONG residues

23: A; 27: C; 33: V; 35: V; 36: V; 37: Y; 46: Y; 48: V; 71: A;
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STRONG

Method: Native exchange in partially folded state by NMR

Conditions: pH 3.0; 25.0 Celsius; Probes: 29

Related publication:
 PMID 8757805

Experiment details: "Redissolving the TFE lyophilisate in 70% TFE, pH 3 results in formation of the TFE state within the dead-time of manual mixing of the CD-monitored kinetics (ca 20 seconds). For bulk exchange experiments the TFE lyophilisate was dissolved in 70% TFE-d3/30% D2O and the pH rapidly adjusted to 3.0 or 4.5. 1D NMR spectra were then consecutively acquired at 25 °C over a period of 16 hours to monitor hydrogen exchange."

Protection threshold: P > 10

Sequence: DTTVSEPAPSCVTLYQSWRYSQADNGCAETVTVKVVYEDDTEGLCYAVAPGQITTVGDGYIGSHGHARYLARCL
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STRONG residues

21: S; 22: Q; 24: D; 27: C; 34: K; 35: V; 36: V; 40: D; 41: T; 42: E; 45: C; 73: C;
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