Protein folding prion

Keywords Prion diseases Prion protein folding Prion strains Prion structural biology Prions... 

Burkhard P, Stetefeld J, Strelkov SV Coiled coils A highly versatile protein folding motif. Trends Cell Biol 2001 11 82. Collinge J Prion diseases of humans and animals Their causes and molecular basis. Annu RevNeurosci 2001 24 519. 

Kelly JW (1998) The environmental dependency of protein folding best explains prion and amyloid diseases. Proc Natl Acad Sci USA 95 930-932. 

Protein Folding Diseases Prion-Induced Dementia... 

Many proteins can be made to clump into fibrous amyloid deposits like those seen in Alzheimer s disease, Creutzfeldt-Jakob disease (the human counterpart of mad cow disease), and other serious ailments. To help prove this point, a natural enzyme to convert to amyloid fibrils—insoluble protein aggregates with a /3-pleated sheet structure—simply by maintaining protein for some time in the unfolded state. Until now, scientists have generally believed that only specific proteins such as amyloid /3-protein and prions are capable of being converted into amyloid fibrils.11 A variety of spectroscopic techniques have been used to confirm the gradual development of amyloid fibrils and to verify the fibrils predominant /3-pleated sheet structure. In the partially unfolded intermediates that form under denaturing conditions, hydrophobic amino acid residues and polypeptide backbone normally buried inside fully folded structures become exposed. Further work is needed to confirm and advance these findings. 

TSEs can exhibit inherited, infectious and sporadic presentations. Additionally, the inherited disease can also be infectious. CJD occurs both as an inherited autosomal dominant disorder and in a transmissible form. In the protein only hypothesis, the abnormal prion protein, either introduced from external sources or produced by the mutated prion protein gene, affects normal protein folding and shifts the prion protein folding towards the formation... 

With the high spatial resolution of the synchrotron, individual cells within a tissue can be probed with subcellular resoluhon. For example, the structures of misfolded protein aggregates in neurological protein folding diseases have been identified in the brain tissue of Alzheimer s disease patients [31-33], while infectious prion proteins have been characterized in scrapie [34-37]. Additional biochemical changes have also been observed in the fingerprint regions of Alzheimer s [38], Parkinson s [39] and scrapie-infected tissues [40]. 

Apetri AC, Maki K, Roder H et al (2006) Early intermediate in human prion protein folding as evidenced by ultrarapid mixing experiments. J Am Chem Soc 128 11673-11678... 

There have been quite a few papers published which deal with fluorescence methods in prion research. Generally, three different approaches have been utilized. First, PrP chimeras with fluorescent proteins (e.g., green fluorescent protein, GFP) have been produced to study various aspects of cellular questions or protein folding. For example, fluorescence imaging techniques have been applied to study prion propagation in yeast (reviewed in [45]). Other examples concern attempts to study protein folding and the nature of aggregates. Kawei-Noma et al. analyzed the... 

Vasiljevic S, Ren J, Yao Y, Dalton K, Adamson CS, Jones IM (2006) Green fluorescent protein as a reporter of prion protein folding. Virol J 3 59... 

Centre for Prions and Protein Folding Diseases, University of Alberta, Edmonton, AB, Canada e-mail david.westaway ualberta.ca... 

The protein-only hypothesis indicates that the scrapie form of the prion protein can promote the conversion of the cellular form. This leads to the conclusion that prions themselves can act as chaperones (Liautard, 1991). Thermokinetic analysis of protein folding shows that a misfolded chaperone gives rise to new misfolded chaperones, which fit very well to the protein-only hypothesis in which PrP triggers the formation of PrP. ... 

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