BMRB Entry 16333

Title:
pH dependent structures of LAH4 in micellar environment: mode of acting
Deposition date:
2009-06-04
Original release date:
2009-11-03
Authors:
Georgescu, Julia; Bechinger, Burkhard
Citation:

Citation: Georgescu, Julia; Bechinger, Burkhard. "Structure-function relationships of the polyhistidine-rich peptide LAH4 in micellar environments; pH dependent mode of antibiotic action & DNA transfection"  Biophys. J. ., .-..

Assembly members:

Assembly members:
LAH4, polymer, 26 residues, 2787.555 Da.

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):
LAH4: KKALLALALHHLAHLALHLA LALKKA

Data sets:
Data typeCount
1H chemical shifts164

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1LAH41

Entities:

Entity 1, LAH4 26 residues - 2787.555 Da.

1   LYSLYSALALEULEUALALEUALALEUHIS
2   HISLEUALAHISLEUALALEUHISLEUALA
3   LEUALALEULYSLYSALA

Samples:

sample_1: lah4 2 mM; H2O 90%; D2O 10%; NaCl 115 mM; Na2HPO4 20 mM; KH2PO4 8 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.8; pressure: 1 atm; temperature: 317 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D DQF-COSYsample_1isotropicsample_conditions_1
2D roesysample_1isotropicsample_conditions_1

Software:

ccnmr, Bruker Biospin, Brunger, Adams, Clore, Gros, Nilges and Read, Cieslar C. et al, Koradi, Billeter and Wuthrich, Laskowski and MacArthur, Rullmann, Doreleijers and Kaptein - chemical shift assignment, data analysis, data analysis, processing, structure solution, visualisation

NMR spectrometers:

  • Bruker DRX 500 MHz

Related Database Links:

BMRB 16332
PDB