BMRB Entry 4723
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR4723
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Title: Involvement of Electrostatic Interactions in the Mechanism of Peptide Folding Induced by Sodium Dodecyl Sulfate Binding
Deposition date: 2000-04-20 Original release date: 2000-05-08
Authors: Montserret, Roland; Mc Leish, Michael; Bockmann, Anja; Geourjon, Christophe; Penin, Francois
Citation: Montserret, Roland; Mc Leish, Michael; Bockmann, Anja; Geourjon, Christophe; Penin, Francois. "Involvement of Electrostatic Interactions in the Mechanism of Peptide Folding Induced by Sodium Dodecyl Sulfate Binding" Biochemistry ., .-. (2000).
Assembly members:
acidic peptide, polymer, 15 residues, Formula weight is not available
Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
acidic peptide: QAPAYEEAAEELAKS
- assigned_chemical_shifts
- coupling_constants
| Data type | Count |
| 13C chemical shifts | 47 |
| 1H chemical shifts | 97 |
| coupling constants | 8 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | acidic peptide | 1 |
Entities:
Entity 1, acidic peptide 15 residues - Formula weight is not available
| 1 | GLN | ALA | PRO | ALA | TYR | GLU | GLU | ALA | ALA | GLU | ||||
| 2 | GLU | LEU | ALA | LYS | SER |
Samples:
sample_1: acidic peptide 11.2 mM; water 50%; CF3CD2OH, [U-2H], 50%; Na phosphate buffer 10 mM
condition_1: pH: 6.0; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| DQF-COSY | not available | not available | not available |
| clean-TOCSY | not available | not available | not available |
| NOESY | not available | not available | not available |
| ROESY | not available | not available | not available |
| 1H-13C-gHSQC | not available | not available | not available |
| gHSQC-TOCSY | not available | not available | not available |
Software:
VNMR v5.1 - peak assignments, processing
NMR spectrometers:
- Varian Unity Plus 500 MHz
Related Database Links:
| PDB |