BMRB Entry 25317

Title:
pH-dependent random coil 1H, 13C, and 15N chemical shifts of the ionizable amino acids: a guide for protein pKa measurements
Deposition date:
2014-10-22
Original release date:
2014-12-09
Authors:
McIntosh, Lawrence; Platzer, Gerald; Okon, Mark
Citation:

Citation: Platzer, Gerald; Okon, Mark; McIntosh, Lawrence. "pH-dependent random coil 1H, 13C, and 15N chemical shifts of the ionizable amino acids: a guide for protein pKa measurements"  J. Biomol. NMR 60, 109-129 (2014).
PubMed: 25239571

Assembly members:

Assembly members:
ACE-GLY-ASP-GLY-NH2 peptide, polymer, 5 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):
ACE-GLY-ASP-GLY-NH2 peptide: XGDGX

Data sets:
Data typeCount
pKa values24
pH NMR parameter values201

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ACE-GLY-ASP-GLY-NH2 peptide1

Entities:

Entity 1, ACE-GLY-ASP-GLY-NH2 peptide 5 residues - Formula weight is not available

1   ACEGLYASPGLYNH2

Samples:

sample_1: blocked tripeptide, [U-13C; U-15N], 10 mM; NaCl 50 mM

sample_conditions_1: temperature: 298 K; pH: 7; pressure: 1 atm; ionic strength: 50 mM

Experiments:

NameSampleSample stateSample conditions
1D 1H-NMRsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
multiple-bond 13C HMBCsample_1isotropicsample_conditions_1
multiple-bond 15N HMBCsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3, Bruker Biospin - chemical shift assignment, data analysis

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz