Amyloid beta: Difference between revisions

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==Structure==
==Structure==
Amyoloid beta is actually the <scene name='Amyloid_beta/C-term/1'>C-terminal</scene> of the <scene name='Amyloid_beta/App/1'>Amyloid Precursor Protein</scene> which  is a type I membrane-spanning glycoprotein [[http://proteopedia.org/wiki/index.php/Amyloid_precursor_protein APP]].<ref name="alz" />  
Amyoloid beta is actually the <scene name='Amyloid_beta/C-term/1'>C-terminal</scene> of the <scene name='Amyloid_beta/App/1'>Amyloid Precursor Protein</scene> which  is a type I membrane-spanning glycoprotein encoded on chromosome 21 [[http://proteopedia.org/wiki/index.php/Amyloid_precursor_protein APP]].<ref name="alz" /> Amyloid beta results from an abnormal cleavage by beta-secretase at the N-terminal and gamma-secretase at the C-terminal. The cleavage is nonspecific and results in peptides 39-43 amino acids in length, with 42 being the most common. Such cleavages occur most commonly in the plasma membrane is also occurs in neuronal membranes.<ref name="alz" /> 
 
The most reasonable structure determined structure consists of <scene name='Amyloid_beta/Two_helices/1'>two helices</scene>; the first helix (residues 8-25) is well defined and has an RMSD of 0.38 angstroms and the second (residues 28-38) is interrupted at the Ile32-Gly33 connection. The two helices are connected by a <scene name='Amyloid_beta/Kink/1'>kink</scene> (residues 26 and 27).<ref name="structure" />
The most reasonable structure determined structure consists of <scene name='Amyloid_beta/Two_helices/1'>two helices</scene>; the first helix (residues 8-25) is well defined and has an RMSD of 0.38 angstroms and the second (residues 28-38) is interrupted at the Ile32-Gly33 connection. The two helices are connected by a <scene name='Amyloid_beta/Kink/1'>kink</scene> (residues 26 and 27).<ref name="structure" />


==References==
==References==
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Laura Olney, Michal Harel, Alexander Berchansky