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Information Journal Paper

Title

INTRODUCING CRITICAL RESIDUES IN THE HUMAN PRION PROTEIN AND ITS ASP 178 ASN MUTANT BY MOLECULAR DYNAMICS SIMULATION

Pages

  153-157

Abstract

 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 kjmol-1nm-2 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.

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    • Cite

    APA: Copy

    MANSOURI, S.. (2011). INTRODUCING CRITICAL RESIDUES IN THE HUMAN PRION PROTEIN AND ITS ASP 178 ASN MUTANT BY MOLECULAR DYNAMICS SIMULATION. JOURNAL OF PHYSICAL AND THEORETICAL CHEMISTRY, 8(2), 153-157. SID. https://sid.ir/paper/569997/en

    Vancouver: Copy

    MANSOURI S.. INTRODUCING CRITICAL RESIDUES IN THE HUMAN PRION PROTEIN AND ITS ASP 178 ASN MUTANT BY MOLECULAR DYNAMICS SIMULATION. JOURNAL OF PHYSICAL AND THEORETICAL CHEMISTRY[Internet]. 2011;8(2):153-157. Available from: https://sid.ir/paper/569997/en

    IEEE: Copy

    S. MANSOURI, “INTRODUCING CRITICAL RESIDUES IN THE HUMAN PRION PROTEIN AND ITS ASP 178 ASN MUTANT BY MOLECULAR DYNAMICS SIMULATION,” JOURNAL OF PHYSICAL AND THEORETICAL CHEMISTRY, vol. 8, no. 2, pp. 153–157, 2011, [Online]. Available: https://sid.ir/paper/569997/en

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