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• W2143331569 abstract "Amyloid formation is dependent to a considerable extent on the amino acid sequence of the protein. The present study delineates certain sequence-dependent features that are correlated with amyloidogenic propensity. The analyses indicate that amyloid formation is favored by lower thermostability and increased half-life of the protein. There seems to be a certain degree of bias in the composition of order-promoting amino acids in the case of amyloidogenic proteins. Based on these parameters, a prediction function for the amyloidogenic propensity of proteins has been created. The prediction function has been found to rationalize the reported effect of certain mutations on amyloid formation. It seems that a higher sheet propensity of residues that constitute the first seven residues of a helical structure in a protein might increase the propensity for a helix to sheet transition in that region under denaturing conditions." @default.
• W2143331569 created "2016-06-24" @default.
• W2143331569 creator A5006668020 @default.
• W2143331569 creator A5053059633 @default.
• W2143331569 date "2005-04-01" @default.
• W2143331569 modified "2023-10-18" @default.
• W2143331569 title "Understanding the relationship between the primary structure of proteins and their amyloidogenic propensity: clues from inclusion body formation" @default.
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• W2143331569 doi "https://doi.org/10.1093/protein/gzi022" @default.
• W2143331569 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15849216" @default.
• W2143331569 hasPublicationYear "2005" @default.
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