Sandbox Reserved 1644: Difference between revisions

Revision as of 17:12, 12 January 2021 view source Camille Spicher (talk \| contribs) 32 edits No edit summary ← Older edit		Revision as of 17:13, 12 January 2021 view source Camille Spicher (talk \| contribs) 32 edits No edit summary Newer edit →
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	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/ ATP].

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