The role of hydrophobicity patterns in prion folding as revealed by recurrence quantification analysis of primary structure.

  • Zbilut J
  • Webber C
  • Colosimo A
 et al. 
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Abstract

It has been suggested that the number and strength of local contacts are the major factors governing conformation accessibility of model two ground-state polypeptide chains. This phenomenology has been posed as a possible factor influencing prion folding. To test this conjecture, recurrence quantification analysis was applied to two model 36mers, and the Syrian hamster prion protein. A unique divergence of the radius function for the recurrence quantification variable %DET of hydrophobicity patterns was observed for both 36mers, and in a critical region of the hamster prion protein. This divergence suggests a partition between strong short- and long-range hydrophobicity patterns, and may be an important factor in prion phenomenology, along with other global thermodynamic factors.

Author-supplied keywords

  • Algorithms
  • Amino Acid Sequence
  • Animals
  • Computer Simulation
  • Cricetinae
  • Mesocricetus
  • Models, Chemical
  • Molecular Sequence Data
  • Prions
  • Prions: chemistry
  • Protein Folding
  • Recombinant Proteins
  • Recombinant Proteins: chemistry

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  • SGR: 0034112880
  • PMID: 10708648
  • SCOPUS: 2-s2.0-0034112880
  • PUI: 30151040
  • ISSN: 0269-2139

Authors

  • J P Zbilut

  • C L Webber

  • a Colosimo

  • a Giuliani

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