Sandbox Reserved 200: Difference between revisions
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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 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. | ||
