NR AMYH
AU Zbilut,J.P.; Webber,C.L.Jr.; Colosimo,A.; Giuliani,A.
TI The role of hydrophobicity patterns in prion folding as revealed by recurrence quantification analysis of primary structure
QU Protein Engineering 2000 Feb; 13(2): 99-104
PT journal article
AB 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.
MH Algorithms; Amino Acid Sequence; Animal; Computer Simulation; Hamsters; Mesocricetus; Models, Chemical; Molecular Sequence Data; Prions/*chemistry; *Protein Folding; Recombinant Proteins/chemistry
AD Department of Molecular Biophysics and Physiology, Rush Medical College, 1653 W. Congress, Chicago, IL 60612, USA. jzbilut@rush.edu
SP englisch
PO England