BMRB Entry 4724

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR4724

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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:

2000-05-09

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:

assigned_chemical_shifts
- chemical_shifts_1
- chemical_shifts_2
coupling_constants
- coupling_constants

Data type	Count
13C chemical shifts	86
1H chemical shifts	218
coupling constants	10

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	basic peptide	1

Entities:

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

1

GLN

ALA

PRO

ALA

TYR

LYS

ALA

LYS

2

LYS

LEU

ALA

GLU

SER

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:

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 - processing peak assignments

NMR spectrometers:

Varian Unity Plus 500 MHz