HIGHLIGHTS
- who: Hugo Fraga from the (UNIVERSITY) have published the paper: Disulfide driven folding for a conditionally disordered protein, in the Journal: (JOURNAL) of 23/Nov/2017
- what: The authors characterize the disorder-to-order transition of a Mia40 substrate, the human small copper chaperone Cox17. Using an integrated real-time approach, including chromatography, fluorescence, CD, FTIR, SAXS, NMR, and MS analysis, the authors demonstrate that in this mitochondrial protein, the conformational switch between disordered and folded states is controlled by the formation of a single disulfide bond, both in the presence and in the absence . . .
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