Molecular dynamics as an approach to study prion protein misfolding and the effect of pathogenic mutations

Marc W van der Kamp, Valerie Daggett

Research output: Contribution to journalArticle (Academic Journal)peer-review

25 Citations (Scopus)
391 Downloads (Pure)

Abstract

Computer simulation of protein dynamics offers unique high-resolution information that complements experiment. Using experimentally derived structures of the natively folded prion protein (PrP), physically realistic dynamics and conformational changes can be simulated, including the initial steps of misfolding. By introducing mutations in silico, the effect of pathogenic mutations on PrP conformation and dynamics can be assessed. Here, we briefly introduce molecular dynamics methods and review the application of molecular dynamics simulations to obtain insight into various aspects of the PrP, including the mechanism of misfolding, the response to changes in the environment, and the influence of disease-related mutations.
Original languageEnglish
Pages (from-to)169-97
Number of pages29
JournalCurrent Topics in Medical Chemistry
Volume305
DOIs
Publication statusPublished - 2011

Keywords

  • Software
  • Animals
  • Protein Structure, Secondary
  • Recombinant Proteins
  • Models, Molecular
  • Humans
  • Hydrogen-Ion Concentration
  • Protein Denaturation
  • Molecular Dynamics Simulation
  • Prions
  • Magnetic Resonance Spectroscopy
  • Protein Folding
  • Prion Diseases
  • Mutation
  • Protein Conformation

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