Sasaki, Ken and Gaikwad, Jyoti and Hashiguchi, Shuhei and Kubota, Toshiya and Sugimura, Kazuhisa and Kremer, Werner and Kalbitzer, Hans Robert and Akasaka, Kazuyuki (2008) Reversible monomer-oligomer transition in human prion protein. PRION, 2 (3). pp. 118-122. ISSN 1933-6896, 1933-690X
Full text not available from this repository. (Request a copy)Abstract
The structure and the dissociation reaction of oligomers PrPoligo from reduced human prion huPrP(C)(23-231) have been studied by H-1-NMR and tryptophan fluorescence spectroscopy at varying pressure, along with circular dichroism and atomic force microscopy. The H-1-NMR and fluorescence spectral feature of the oligomer is consistent with the notion that the N-terminal residues including all seven Trp residues, are free and mobile, while residues 105 similar to 210, comprising the AGAAAAGA motif and S1-Loop-HelixA-Loop-S2-Loop-HelixC, are engaged in intra- and/or inter-molecular interactions. By increasing pressure to 200 MPa, the oligomers tend to dissociate into monomers which may be identified with PrPC*, a rare metastable form of PrPC stabilized at high pressure (Kachel et al., BMC Struct Biol 6: 16). The results strongly suggest that the oligomeric form PrPoligo is in dynamic equilibrium with the monomeric forms via PrPC*, namely huPrP(C) reversible arrow huPrP(C)* reversible arrow huPrP(oligo).
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | PRESSURE NMR-SPECTROSCOPY; INTERMEDIATE STATES; CONVERSION; DISSOCIATION; PRPSC; human prion; oligomer structure; pressure dissociation; reversible monomer-oligomer transition; circular dichroism; high pressure NMR; atomic force microscopy |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 29 Oct 2020 06:04 |
| Last Modified: | 29 Oct 2020 06:04 |
| URI: | https://pred.uni-regensburg.de/id/eprint/30711 |
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