Sandbox Reserved 815: Difference between revisions
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== Repercussion of the M129/V129 polymorphism == | == Repercussion of the M129/V129 polymorphism == | ||
It’s known that the transformation of the normal protein in its infectious model involves a conversion from a soluble and predominantly α-helical protein to an aggregated form, which is substantially enriched in β-sheet. | It’s known that the transformation of the normal protein in its infectious model involves a conversion from a soluble and predominantly α-helical protein to an aggregated form, which is substantially enriched in β-sheet. | ||
The substitution by a valine at residue 129 influences intermolecular beta-sheet formation and conformation. Even if the structure is not distorted by the substitution (no effect on the stability, folding, or dynamics), the difference is based on the interaction by the beta-sheet between two dimers. With two M129 dimers, there is an identical and stable intermolecular 129-130 beta-sheet interaction. However with two V129 variant dimers, it appears a flexion, form to prevent steric troubles between them. In some cases of variants, the beta-sheet interface is entirely absent. This tendency allows the exposure of beta-sheet to the exterior of the protein and thus occasionally influences the aggregation form and so the development of prions. | The substitution by a valine at residue 129 influences intermolecular beta-sheet formation and conformation. Even if the structure is not distorted by the substitution (no effect on the stability, folding, or dynamics), the difference is based on the interaction by the beta-sheet between two dimers. With two M129 dimers, there is an identical and stable intermolecular 129-130 beta-sheet interaction. However with two V129 variant dimers, it appears a flexion, form to prevent steric troubles between them. In some cases of variants, the beta-sheet interface is entirely absent. This tendency allows [C:\Users\Pierre-Yves\Desktop\Dimérisation.jpg the exposure of beta-sheet to the exterior of the protein] and thus occasionally influences the aggregation form and so the development of prions. | ||
The common Methionine/Valine polymorphism residue in 129 in the PrP influences disease. | The common Methionine/Valine polymorphism residue in 129 in the PrP influences disease. | ||
