Structural region essential for amyloid fibril formation in cytochrome c elucidated by optical trapping.

Shun HirotaChun-Liang ChiuChieh-Ju ChangPei-Hua LoTien ChenHongxu YangMasaru YamanakaTsuyoshi Mashima Cheng Xie Hiroshi Masuhara Teruki Sugiyama

Published in: Chemical communications (Cambridge, England) (2022)

Amyloid fibril formation of cytochrome c is spatially and temporally controlled with a combined method of disulfide bond cross-linking of cysteine-introduced variants and optical trapping, identifying that the structural change in the region containing Ala83 is essential for the amyloid fibril formation.

Keyphrases

high resolution
high speed
copy number
dna methylation
transition metal