Protein Variants | Comment | Organism |
---|---|---|
additional information | the native state of the enzyme presents two alpha-helices. Equilibrium and kinetic measurements for folding indicate that only helix-2, spanning residues 55-67, is largely stabilized in the transition state for folding therfore playing a relevant role in this process. The aggregation rate appears to vary only for the variants in which the propensity of the region corresponding to helix-1, spanning residues 22-32, is changed. Mutations that stabilize the first helix slow down the aggregation process while those that destabilize it increase the aggregation rate | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
muscle | - |
Homo sapiens | - |