BMRB Entry 4724

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:
2000-05-09
Authors:
Montserret, Roland; Mc Leish, Michael; Bockmann, Anja; Geourjon, Christophe; Penin, Francois
Citation:

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:

Assembly members:
basic peptide, polymer, 15 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
basic peptide: QAPAYKKAAKKLAES

Data sets:
Data typeCount
13C chemical shifts86
1H chemical shifts218
coupling constants10

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1basic peptide1

Entities:

Entity 1, basic peptide 15 residues - Formula weight is not available

1   GLNALAPROALATYRLYSLYSALAALALYS
2   LYSLEUALAGLUSER

Samples:

sample_1: basic peptide 10.4 mM; water 50%; CF3CD2OH, [U-2H], 50%; Na phosphate buffer 10 mM

sample_2: basic peptide 11.0 mM; Na dodecyl sulfate buffer, [U-2H], 40 mM; Na phosphate buffer 10 mM

condition_1: pH: 6.0; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
DQF-COSYnot availablenot availablenot available
clean-TOCSYnot availablenot availablenot available
NOESYnot availablenot availablenot available
ROESYnot availablenot availablenot available
1H-13C-gHSQCnot availablenot availablenot available
gHSQC-TOCSYnot availablenot availablenot available

Software:

VNMR v5.1 - processing peak assignments

NMR spectrometers:

  • Varian Unity Plus 500 MHz

Related Database Links:

PDB