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• W4382137668 endingPage "10613" @default.
• W4382137668 startingPage "10613" @default.
• W4382137668 abstract "Amyloid formation is a hallmark of various neurodegenerative disorders. In this contribution, energy landscapes are explored for various hexapeptides that are known to form amyloids. Heat capacity (CV) analysis at low temperature for these hexapeptides reveals that the low energy structures contributing to the first heat capacity feature above a threshold temperature exhibit a variety of backbone conformations for amyloid-forming monomers. The corresponding control sequences do not exhibit such structural polymorphism, as diagnosed via end-to-end distance and a dihedral angle defined for the monomer. A similar heat capacity analysis for dimer conformations obtained using basin-hopping global optimisation shows clear features in end-to-end distance versus dihedral correlation plots, where amyloid-forming sequences exhibit a preference for larger end-to-end distances and larger positive dihedrals. These results hold true for sequences taken from tau, amylin, insulin A chain, a de novo designed peptide, and various control sequences. While there is a little overall correlation between the aggregation propensity and the temperature at which the low-temperature CV feature occurs, further analysis suggests that the amyloid-forming sequences exhibit the key CV feature at a lower temperature compared to control sequences derived from the same protein." @default.
• W4382137668 created "2023-06-27" @default.
• W4382137668 creator A5014057135 @default.
• W4382137668 creator A5022301289 @default.
• W4382137668 date "2023-06-25" @default.
• W4382137668 modified "2023-09-30" @default.
• W4382137668 title "Energy Landscapes and Heat Capacity Signatures for Monomers and Dimers of Amyloid-Forming Hexapeptides" @default.
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• W4382137668 doi "https://doi.org/10.3390/ijms241310613" @default.
• W4382137668 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/37445791" @default.
• W4382137668 hasPublicationYear "2023" @default.
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