BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 888

Title: pH-Induced Denaturation of Proteins: A Single Salt Bridge Contributes 3-5 kcal/mol to the Free Energy of Folding of T4 Lysozyme

Deposition date: 1995-07-31 Original release date: 1995-07-31

Authors: Anderson, D.; Becktel, Wayne; Dahlquist, Frederick

Citation: Anderson, D.; Becktel, Wayne; Dahlquist, Frederick. "pH-Induced Denaturation of Proteins: A Single Salt Bridge Contributes 3-5 kcal/mol to the Free Energy of Folding of T4 Lysozyme"  Biochemistry 29, 2403-2408 (1990).

Assembly members:
lysozyme, polymer, 97 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: not available

Entity Sequences (FASTA):
lysozyme: XXXXXXXXXXXXXXXXXXXX XXXXXXXXXXHXXXXXXXXX XXXXXXXXXXXXXTXXXXXX XXXXXXXXXDXXXXXXXXXX XXXXXXXXXXXXXXXXA

Data sets:
Data typeCount
1H chemical shifts1

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1lysozyme1

Entities:

Entity 1, lysozyme 97 residues - Formula weight is not available

1   XXXXXXXXXX
2   XXXXXXXXXX
3   XXXXXXXXXX
4   HISXXXXXXXXX
5   XXXXXXXXXX
6   XXXTHRXXXXXX
7   XXXXXXXXXASP
8   XXXXXXXXXX
9   XXXXXXXXXX
10   XXXXXXALA

Samples:

sample_one:

sample_condition_set_one: pH: 5.95 na; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
unknownsample_oneisotropicsample_condition_set_one

Software:

No software information available

NMR spectrometers:

  • unknown unknown 0 MHz