Human Prion Protein Dimer: Difference between revisions
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<StructureSection load='1i4m' size='300' side='left' caption='Major Prion Protein: Dimerized [[1I4M]]' scene=''> | <StructureSection load='1i4m' size='300' side='left' caption='Major Prion Protein: Dimerized [[1I4M]]' scene=''> | ||
The <scene name='User:Erin_May/Sandbox_1/Previously_shown_residues/1'>residues</scene>, shown above, alter the function of Major Prion Protein's ability to re-fold, however their positions on the wild-type monomer and fully unfolded PrP<sup>Sc</sup>, do not illustrate a clear mechanism for propagation. The dimer brings light to these residues influence on the infectious qualities of the disease causing residues. | The <scene name='User:Erin_May/Sandbox_1/Previously_shown_residues/1'>residues</scene>, shown above, alter the function of Major Prion Protein's ability to re-fold, however their positions on the wild-type monomer and fully unfolded PrP<sup>Sc</sup>, do not illustrate a clear mechanism for propagation. The dimer brings light to these residues' influence on the infectious qualities of the disease causing residues. | ||
It is theorized from this dimeric structure that the dimerization is the first step in amyloid formation and the presence of these dimers could possibly speed up the aggregation of PrP<sup>Sc</sup>. | It is theorized from this dimeric structure that the dimerization is the first step in amyloid formation and the presence of these dimers could possibly speed up the aggregation of PrP<sup>Sc</sup>. | ||
