Application | Comment | Organism |
---|---|---|
additional information | submolecular mechanism of amyloid formation based on a model system of PGK, evaluated by microscopic measurements and tryptophan fluorescence. Interactions between the polypeptide chains of the two domains of the protein direct the misfolding process from the early steps to the amyloid formation, and influence the final structure. Kinetics of misfolding is different for the individual domains. Misfolding of the domains within the complete protein is synchronized indicating that domain-domain interactions direct the misfolding and amyloid formation mechanism | Saccharomyces cerevisiae |
Protein Variants | Comment | Organism |
---|---|---|
additional information | mutants HisN W122, HisC W333, His-PGK W122, and His-PGK W333, single tryptophan mutants of the individual N and C terminal domains and the complete protein, amyloid fibrils grow from all mutants under identical conditions as for the wild-type protein | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Saccharomyces cerevisiae |
Storage Stability | Organism |
---|---|
-80°C, 50 mM phosphate buffer, pH 6.2 | Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
PGK | - |
Saccharomyces cerevisiae |