Conformational Stability of PrP Amyloid Fibrils Controls Their Smallest Possible Fragment Size
نویسندگان
چکیده
منابع مشابه
A Molecular Dynamics study on the conformational stability of PrP 180 - 193 Helix II Prion fragment
Molecular Dynamics of PrP 180-193 has allowed us to investigate the stability of the α-helical conformation of the zwitterionic peptide (L1) and the neutralized (L2). In water, the helical structure of L1, is unstable; in L2, the α-helix breaks up in the middle at Gln186, and the two resulting connected helices are stable. The hydrophobic enviroment decreases the stability of the helical struct...
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BACKGROUND According to the prevailing view, soluble oligomers or small fibrillar fragments are considered to be the most toxic species in prion diseases. To test this hypothesis, two conformationally different amyloid states were produced from the same highly pure recombinant full-length prion protein (rPrP). The cytotoxic potential of intact fibrils and fibrillar fragments generated by sonica...
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ژورنال
عنوان ژورنال: Journal of Molecular Biology
سال: 2008
ISSN: 0022-2836
DOI: 10.1016/j.jmb.2007.12.053