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Abstract: The prion protein is a copper binding glycoprotein that in mammals can misfold into a pathogenic isoform leading to prion diseases, as opposed, surprisingly, to avians. The avian prion N-terminal tandem repeat is richer in prolines than the mammal one, and understanding their effect on conformation is of great biological importance. Here we succeeded in investigating the conformations of a single avian hexarepeat by means of NMR and molecular dynamics techniques. We found a high flexibility and a strong conformational dependence on pH: local turns are present at acidic and neutral pH, while unordered regions dominate at basic conditions. [Copyright &y& Elsevier]

The effects of the cis and trans form of the 4-OMe-phenylazobenzene at 1% and 7% mole fraction on order, mesophase stability and dynamics of the 5CB liquid crystal were studied using the ESR spin probe technique. The presence of the trans azo-derivative induced a downshift of the nematic-isotropic transition temperature TNI which increased with the concentration but did not change the dependence of the order parameter on the reduced temperature. The cis isomer caused even larger TNI shifts, determining a marked decrease of the order parameter with a peculiar dependence on the reduced temperature, quite different from the standard Haller-type behavior. The spin probe dynamics appeared instead to be essentially unchanged by the presence of the azo-derivative. [ABSTRACT FROM AUTHOR]