شماره ركورد كنفرانس :
3834
عنوان مقاله :
Effect of Familial Mutations on Salt-Bridge Formation in Aβ42 Monomers
پديدآورندگان :
Aghayari Mohsen M.aghayari1989@yahoo.com Department of Physical Chemistry, Chemistry and Chemical Engineering Research Center of Iran, Tehran, Iran; , Karimi-Jafari Mohammad Hossein mhkarimijafari@ut.ac.ir Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran; , Firouzi Rouhollah Department of Physical Chemistry, Chemistry and Chemical Engineering Research Center of Iran, Tehran, Iran
كليدواژه :
amyloid , beta , salt , bidge , simulated annealing
عنوان كنفرانس :
نوزدهمين سمينار شيمي فيزيك ايران
چكيده فارسي :
Recent experimental and computational studies suggest that there is a U-shape motif in the middle region (20-30) of Aβ monomers that is stabilized by salt bridges between residues Glu22/Asp23 (as the anions) and Lys28 (as the cation). It seems that the competition between two anionic residues (D23 and E22) to make the salt-bridge with the Lys28, can be considered as a controlling parameter in yielding a Aβ42 monomer with the U-shaped conformation. Consequently, by replacing each of these anionic residues with neutral residues containing small side-chain (such as Gly, in E22G) the salt-bridges formation between residues Glu22/Asp23 and Lys28 is facilitated.
