Start2Fold

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

Entry STF0053

G. gallus alpha-spectrin SH3

 DOWNLOAD ENTRY IN XML

Protein information

Name of the protein: Spectrin alpha chain, non-erythrocytic 1
Organism: Gallus gallus (Chicken)
Number of residues: 62
Related UniProt entry:   P07751 (Fragment: 964 - 1025)
Related PDB entry:   1SHG

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

 Show  Hide

STRONG

Method: Native exchange NMR

Conditions: pH 4.0; 25.0 Celsius; Probes: 36

Related publication:
 PMID 10413463

Experiment details: "H-D exchange was initiated by rapidly dissolving the lyophilized protein in deuterated buffer (20 mM d5-glycine for pH* 3.0 and pH* 2.5 or 20 mM d3-acetate for pH* 4.0). The sample was filtered to remove insoluble protein, and then immediately placed in a 5 mm NMR tube and into the magnet. The final protein concentration was approximately 5 mM when dissolved in 500 µL of deuterated buffer. The pH* of samples was checked after each experiment. Values of pH* reported in D2O solutions represent direct pH meter readings, without correction for isotope effects. The experiment dead times (i.e., time between dissolving the protein and the start of data acquisition) were between 15 and 20 min."

Protection threshold: ln(P) > 4

Sequence: MDETGKELVLALYDYQEKSPREVTMKKGDILTLLNSTNKDWWKVEVNDRQGFVPAAYVKKLD
 CLICK TO DOWNLOAD SEQUENCE IN FASTA

STRONG residues

9: V; 10: L; 11: A; 12: L; 13: Y; 15: Y; 25: M; 26: K; 28: G; 31: L; 32: T; 33: L; 34: L; 42: W; 43: K; 44: V; 45: E; 51: G; 52: F; 53: V; 55: A; 57: Y; 58: V; 59: K;
 CLICK TO DOWNLOAD LIST OF RESIDUES

 Show  Hide

MEDIUM

Method: Native exchange NMR

Conditions: pH 4.0; 25.0 Celsius; Probes: 36

Related publication:
 PMID 10413463

Experiment details: "H-D exchange was initiated by rapidly dissolving the lyophilized protein in deuterated buffer (20 mM d5-glycine for pH* 3.0 and pH* 2.5 or 20 mM d3-acetate for pH* 4.0). The sample was filtered to remove insoluble protein, and then immediately placed in a 5 mm NMR tube and into the magnet. The final protein concentration was approximately 5 mM when dissolved in 500 µL of deuterated buffer. The pH* of samples was checked after each experiment. Values of pH* reported in D2O solutions represent direct pH meter readings, without correction for isotope effects. The experiment dead times (i.e., time between dissolving the protein and the start of data acquisition) were between 15 and 20 min."

Protection threshold: 2 < ln(P) < 4

Sequence: MDETGKELVLALYDYQEKSPREVTMKKGDILTLLNSTNKDWWKVEVNDRQGFVPAAYVKKLD
 CLICK TO DOWNLOAD SEQUENCE IN FASTA

MEDIUM residues

8: L; 16: Q; 22: E; 23: V; 24: T; 30: I; 41: W; 61: L;
 CLICK TO DOWNLOAD LIST OF RESIDUES