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- W3035263592 endingPage "1257" @default.
- W3035263592 startingPage "1253" @default.
- W3035263592 abstract "Shedding light on disordered proteins Disordered proteins often fold as they bind to a partner protein. There could be many different molecular trajectories between the unbound proteins and the bound complex. Most methods to measure transition paths rely on monitoring a single distance, making it difficult to resolve complex pathways. Kim and Chung used fast three-color single-molecule Foster resonance energy transfer (FRET) to simultaneously probe distance changes between the two ends of an unfolded protein and between each end and a probe on the partner protein. They show that binding can be initiated by diverse conformations and that the molecules are held together by non-native interactions as the disordered protein folds. This allows the association to be diffusion limited because most collisions lead to binding. Science , this issue p. 1253" @default.
- W3035263592 created "2020-06-19" @default.
- W3035263592 creator A5083376970 @default.
- W3035263592 creator A5086015881 @default.
- W3035263592 date "2020-06-12" @default.
- W3035263592 modified "2023-09-25" @default.
- W3035263592 title "Disordered proteins follow diverse transition paths as they fold and bind to a partner" @default.
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- W3035263592 doi "https://doi.org/10.1126/science.aba3854" @default.
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