The molecular dynamics (MD) simulation method is used to assess structural details for human prion protein (hereafter PrPN) and its Asp178 Asn mutant (hereafter PrPm) which causes fatal familial insomnia disease. The results reveal that the flexibility and instability increase in PrPm could be related to specific amino acids exposed to the solvent. Solvation free energy of PrPm is 20 kjmot1nni2 more than PrPN that is caused by solvent accessible surface area (SASA) especially hydrophobic area, Spho. The study of time interval properties indicates a number of critical amino acids in prion proteins, which exposed to the solvent. They can be ideal anchor-points for initial intermolecular contacts, or affect metal-ion occupancy. The present achievements may be used in drug design for the prevention or treatment of disease..
Mansouri, S. (2011). Introducing critical residues in the human prion protein and its Asp 178 Asn mutant by molecular dynamics simulation. Journal of Physical & Theoretical Chemistry, 8(2), 75-80.
MLA
S. Mansouri. "Introducing critical residues in the human prion protein and its Asp 178 Asn mutant by molecular dynamics simulation". Journal of Physical & Theoretical Chemistry, 8, 2, 2011, 75-80.
HARVARD
Mansouri, S. (2011). 'Introducing critical residues in the human prion protein and its Asp 178 Asn mutant by molecular dynamics simulation', Journal of Physical & Theoretical Chemistry, 8(2), pp. 75-80.
VANCOUVER
Mansouri, S. Introducing critical residues in the human prion protein and its Asp 178 Asn mutant by molecular dynamics simulation. Journal of Physical & Theoretical Chemistry, 2011; 8(2): 75-80.
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