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• W2057165514 endingPage "285225" @default.
• W2057165514 startingPage "285225" @default.
• W2057165514 abstract "The determination of factors that influence conformational changes in proteins is very important for the identification of potentially amyloidogenic and disordered regions in polypeptide chains. In our work we introduce a new parameter, mean packing density, to detect both amyloidogenic and disordered regions in a protein sequence. It has been shown that regions with strong expected packing density are responsible for amyloid formation. Our predictions are consistent with known disease-related amyloidogenic regions for 9 of 12 amyloid-forming proteins and peptides in which the positions of amyloidogenic regions have been revealed experimentally. Our findings support the concept that the mechanism of formation of amyloid fibrils is similar for different peptides and proteins. Moreover, we have demonstrated that regions with weak expected packing density are responsible for the appearance of disordered regions. Our method has been tested on datasets of globular proteins and long disordered protein segments, and it shows improved performance over other widely used methods. Thus, we demonstrate that the expected packing density is a useful value for predicting both disordered and amyloidogenic regions of a protein based on sequence alone. Our results are important for understanding the structural characteristics of protein folding and misfolding." @default.
• W2057165514 created "2016-06-24" @default.
• W2057165514 creator A5001775435 @default.
• W2057165514 creator A5023828983 @default.
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• W2057165514 date "2007-06-25" @default.
• W2057165514 modified "2023-10-18" @default.
• W2057165514 title "Expected packing density allows prediction of both amyloidogenic and disordered regions in protein chains" @default.
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• W2057165514 doi "https://doi.org/10.1088/0953-8984/19/28/285225" @default.
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