The structure and the dissociation reaction of oligomers PrP oligo from reduced human prion huPrP C (23-231) have been studied by 1 H-NMR and tryptophan fluorescence spectroscopy at varying pressure, along with circular dichroism and atomic force microscopy. The 1 H-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 105~210, 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 PrP C* , a rare metastable form of PrP C stabilized at high pressure (Kachel et al., BMC Struct Biol 6:16). The results strongly suggest that the oligomeric form PrP oligo is in dynamic equilibrium with the monomeric forms via PrP C* , namely huPrP C  huPrP C*  huPrP oligo .

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Protein expression by using cell − based method 【norma 川y needs tedieus optimization since conditions Leading to the production of higll yield