Fig. 2: VQIVYK is essential in S320F facilitated aggregation, and the surrounding sequence regulates aggregation. | Nature Communications

Fig. 2: VQIVYK is essential in S320F facilitated aggregation, and the surrounding sequence regulates aggregation.

From: FTD-tau S320F mutation stabilizes local structure and allosterically promotes amyloid motif-dependent aggregation

Fig. 2: VQIVYK is essential in S320F facilitated aggregation, and the surrounding sequence regulates aggregation.The alternative text for this image may have been generated using AI.

a Design of sequence fragments encompassing 320 positions in WT or S320F context. The 320 position and 306VQIVYK311 are underlined. b ThT fluorescence signal at 72 h for each sequence fragment of WT (black) and S320F (red). The data are presented as an average t1/2max +/− SD from fits to a non-linear regression model in GraphPad Prism n = 3 biological replicates. c Representative TEM images of each peptide from the ThT assays at 72 h endpoint.

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