| Literature DB >> 10585952 |
C Schladitz1, E P Vieira, H Hermel, H Möhwald.
Abstract
An amyloid(1-40) solution rich in coil, turn, and alpha-helix, but poor in beta-sheet, develops monolayers with a high beta-sheet content when spread at the air-water interface. These monolayers are resistant to repeated compression-dilatation cycles and interaction with trifluoroethanol. The secondary structure motifs were detected by circular dichroism (CD) in solution and with infrared reflection-absorption spectroscopy (IRRAS) at the interface. Hydrophobic influences are discussed for the structure conversion in an effort to understand the completely unknown reason for the natural change of the normal prion protein cellular (PrP(C)) into the abnormal prion protein scrapie (PrP(Sc)).Entities:
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Year: 1999 PMID: 10585952 PMCID: PMC1300601 DOI: 10.1016/S0006-3495(99)77161-4
Source DB: PubMed Journal: Biophys J ISSN: 0006-3495 Impact factor: 4.033