Sandbox Reserved 595: Difference between revisions
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ApoE proteins self-associate in order to form dimers, tetrameters, and higher aggregates. These phenomena occur in a concentration, pH, and temperature-dependent manner (N). Oligomerization also correlates with the length of the C-terminal domain (O). Resulting from this protein's propensity to aggregate is difficulty in determining the full-length three-dimensional structure (P). At μM concentrations, ApoE primarily exists as a tetrameter. When members of a tetrameter dissociate, the subsequent dimeric and monomeric forms retain their structure; dissociation from a tetrameter may serve to open new ligand binding sites (Q). | ApoE proteins self-associate in order to form dimers, tetrameters, and higher aggregates. These phenomena occur in a concentration, pH, and temperature-dependent manner (N). Oligomerization also correlates with the length of the C-terminal domain (O). Resulting from this protein's propensity to aggregate is difficulty in determining the full-length three-dimensional structure (P). At μM concentrations, ApoE primarily exists as a tetrameter. When members of a tetrameter dissociate, the subsequent dimeric and monomeric forms retain their structure; dissociation from a tetrameter may serve to open new ligand binding sites (Q). | ||
=Function= | |||
=Clinical Relevance= | |||
=References= | |||
