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- W3205211474 abstract "Amyloid fibril formation occurs in restricted environment, such as the interface between intercellular fluids and bio-membranes. Conformational interconversion from α-helix to β-structure does not progress in fluids; however, it can occur after sedimentary aggregation during amyloid fibril formation induced by heat treatment of hen egg white lysozyme (HEWL). Secondary structures of various proteins and denatured proteins titrated with 2,2,2-trifluoroethanol (TFE) were examined using their CD spectra. Gaussian peak/trough and singular value decompositions (SVD) showed that the spectral pattern of the α-helix comprised a sharp trough at wavelength 207 nm and a broad trough at 220 nm. Conversely, we distinguished two patterns for β-sheet-a spread barrel type, corresponding to ConA, and a tightly weaved type, corresponding to the soybean trypsin inhibitor. Herein, we confirmed that the spectral/conformational interconversion of the heat-treated HEWL was not observed in the dissolved fluid." @default.
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- W3205211474 date "2021-12-01" @default.
- W3205211474 modified "2023-10-06" @default.
- W3205211474 title "Singular value decomposition analysis of the secondary structure features contributing to the circular dichroism spectra of model proteins" @default.
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- W3205211474 doi "https://doi.org/10.1016/j.bbrep.2021.101153" @default.
- W3205211474 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8528683" @default.
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