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Rabbits are one of the very few mammals that can resist infectious spongiform encephalopathy (TSE). Studies have shown that the rabbit prion protein (PrPC) is different from most mammalian PrPC. It does not undergo PrPC → PrPSc conformational change, but its molecular mechanism is not yet clear. It is expected to be closely related to the spatial structure and dynamics of rabbit PrPC protein. Related.
In recent years, Lin Donghai's group at the Shanghai Institute of Materia Medica, Chinese Academy of Sciences has used multi-dimensional NMR technology to study the solution structure and dynamics of multiple point mutant proteins such as rabbit PrPC (91-228) and S173N, and found that rabbit PrPC protein has unique characteristics. Spatial structure and dynamic properties. The researchers pointed out that the interaction between loop165-172 and the end of the a3 helix and the unique surface charge distribution may be the main factors that lead to the unique biological function and biochemical properties of rabbit prion protein.
Solution structure of rabbit prion protein and its I173V mutant
The results of this study are helpful to reveal the molecular mechanism of PrPC → PrPSc conformational change of prion protein and the pathogenesis of TSE. The research results were recently published in the Journal of Biochemistry (JBC).
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