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).
=Isoforms=
Three main isoforms exist for human apoE (apoE2, apoE3, apoE4).  They are coded for by three different alleles at the same locus (ε2, ε3, ε4).  These isoforms of apoE were identified through isoelectric focusing and have 0, +1, and +2 charges to account for the electophoretic differences that they display (W). 
==ApoE3==
ApoE is the most frequent form and is thus considered to be the "wildtype" isoform of apoE. 
==ApoE4==
ApoE4 has a higher percentage of randomly coiled structure, a feature that could contribute to its greater tendency to aggregate (F).   


=Function=
=Function=