Misfolded regions

The results of these tests are displayed as bar graphs, where positive values indicate misaligned or misfolded regions and negative values indicate... 

The conformational plasticity supported by mobile regions within native proteins, partially denatured protein states such as molten globules, and natively unfolded proteins underlies many of the conformational (protein misfolding) diseases (Carrell and Lomas, 1997 Dobson et al., 2001). Many of these diseases involve amyloid fibril formation, as in amyloidosis from mutant human lysozymes, neurodegenerative diseases such as Parkinson s and Alzheimer s due to the hbrillogenic propensities of a -synuclein and tau, and the prion encephalopathies such as scrapie, BSE, and new variant Creutzfeldt-Jacob disease (CJD) where amyloid fibril formation is triggered by exposure to the amyloid form of the prion protein. In addition, aggregation of serine protease inhibitors such as a j-antitrypsin is responsible for diseases such as emphysema and cirrhosis. 

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]. 

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