Sandbox Reserved 1644: Difference between revisions
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Lon proteins are therefore an hexameric chambered protease complex. (This structure is similar with yeast [https://www.yeastgenome.org/locus/S000000118 Pim1] ) | Lon proteins are therefore an hexameric chambered protease complex. (This structure is similar with yeast [https://www.yeastgenome.org/locus/S000000118 Pim1] ) | ||
The six Lon monomers are forming three pairs of legs owned by the N-terminal domain of the protein. This structure is emerging of the protein as a trimer of dimers. | The six Lon monomers are forming three pairs of legs owned by the N-terminal domain of the protein. This structure is emerging of the protein as a trimer of dimers. | ||
Like many proteins, Lon is a '''flexible''' peptide which has different '''three-dimensional conformations'''. The protein can therefore pass from one conformation to another by hydrolysis of [https://biologydictionary.net/atp/#:~:text=Adenosine%20triphosphate%2C%20also%20known%20as,%2C%20cellular%20respiration%2C%20and%20fermentation. ATP]. | Like many proteins, Lon is a '''flexible''' peptide which has different '''three-dimensional conformations'''. The protein can therefore pass from one conformation to another by hydrolysis of [https://biologydictionary.net/atp/#:~:text=Adenosine%20triphosphate%2C%20also%20known%20as,%2C%20cellular%20respiration%2C%20and%20fermentation. ATP]. | ||
