Protein Variants | Comment | Organism |
---|---|---|
additional information | differential comparison of the activation domain of the proenzyme with three site-directed mutants of different conformational stability by determination of hydrogen exchange using deuterated MALDI-TOF mass spectrometry, overview | Homo sapiens |
General Stability | Organism |
---|---|
the denaturation with 5 M urea is fully reversible at pH 7.0, the enzyme shows a two state folding transition | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
potato carboxypeptidase inhibitor | determination of hydrogen exchange in the slow exchange core of the inhibitor in different conformational stages using deuterated matrix-assisted laser desorption/ionization time-of-flight mass spectrometry, overview | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Renatured (Comment) | Organism |
---|---|
the denaturation with 5 M urea is fully reversible at pH 7.0, the enzyme shows a two state folding transition | Homo sapiens |
Subunits | Comment | Organism |
---|---|---|
More | differential comparison of the activation domain of the proenzyme with three site-directed mutants of different conformational stability by determination of hydrogen exchange using deuterated MALDI-TOF mass spectrometry, overview | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
ADA2 | - |
Homo sapiens |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
90 | - |
3 h, denturation, wild-type and mutant enzymes, determination of hydrogen exchange, after 30 min at room temperature prior to 10fold dilution with proton containing buffer, two mutants fail to denature | Homo sapiens |