Sandbox Reserved 200: Difference between revisions
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[http://en.wikipedia.org/wiki/Alzheimer%27s_disease Alzheimer’s disease] is a terminal disease that slowly degenerates the brain. One of the possible causes of Alzheimer’s is [http://en.wikipedia.org/wiki/Amyloid amyloid] deposits throughout the brain. Though RNasa A oligomers are not the amyloid deposits that cause Alzheimer’s the folding of these oligomers gives clues towards the formation of amyloid deposits responsible for Alzheimer’s. | [http://en.wikipedia.org/wiki/Alzheimer%27s_disease Alzheimer’s disease] is a terminal disease that slowly degenerates the brain. One of the possible causes of Alzheimer’s is [http://en.wikipedia.org/wiki/Amyloid amyloid] deposits throughout the brain. Though RNasa A oligomers are not the amyloid deposits that cause Alzheimer’s the folding of these oligomers gives clues towards the formation of amyloid deposits responsible for Alzheimer’s. | ||
The 3D domain swapping | |||
The 3D domain swapping has many similarities with the formation of amyloid fibers. Both are highly specific reactions coming from only one type of monomer and these reactions can form linear aggregates. <ref name=”liu01/> These aggregates of proteins are formed by hydrogen bonding at the hinge loops which form an antiparalell β-pleated sheet. <ref name=”liu01/> This most commonly happens with the major dimer. Liu suggests that all proteins are capable of forming aggregates by domain swapping as long as they are in high concentration and partially destabilized. <ref name=”liu01/> As 3D domain swapping becomes more understood, it will offer insight to the amyloid formation in Alzheimer’s patients. | |||
The RNase A 3D swapped oligomers show significant biological activity including allostery, antitumor, and immunorepression activity. This same activity has not observed in the monomer and the non-3D domain swapped dimers .<ref name="liu98">PMID:9502384</ref > This could be due to the fact that the monomer has a cystolic RNase A inhibitor that is unable to inhibit the active sites of the oligomers. <ref name="liu01">PMID:11790847</ref > | The RNase A 3D swapped oligomers show significant biological activity including allostery, antitumor, and immunorepression activity. This same activity has not observed in the monomer and the non-3D domain swapped dimers .<ref name="liu98">PMID:9502384</ref > This could be due to the fact that the monomer has a cystolic RNase A inhibitor that is unable to inhibit the active sites of the oligomers. <ref name="liu01">PMID:11790847</ref > | ||