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Sagot :
Essential aminoacid (Ile) and leucine (Leu) are unit isomers of one another, sharing a great deal in common with their structures and characteristics.
They both have hydrophobic aspect chains that are the same length. In order to minimize interference with the network of water H-bonds caused by the hydrophobic contact, each residue will try to bury itself within the interior of the macromolecule. Leu and Ile will thus be at very similar positions in wild-type and mutant proteins.Essential aminoacid (Ile) and leucine (Leu) are unit isomers of one another, sharing a great deal in common with their structures and characteristics. Since they are isomers, they require similar facet chain geometries so that steric restrictions won't be an issue and they can all occupy a very similar space within the hydrophobic core of the macromolecule. As in the case of the wild type catalyst, Leu is in the situation and is possibly involved in the catalyst's mechanism.
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