Disordered proteins follow diverse transition paths as they fold and bind to a partner.

Science
Jae-Yeol Kim, Hoi Sung Chung

Abstract

Transition paths of macromolecular conformational changes such as protein folding are predicted to be heterogeneous. However, experimental characterization of the diversity of transition paths is extremely challenging because it requires measuring more than one distance during individual transitions. In this work, we used fast three-color single-molecule Förster resonance energy transfer spectroscopy to obtain the distribution of binding transition paths of a disordered protein. About half of the transitions follow a path involving strong non-native electrostatic interactions, resulting in a transition time of 300 to 800 microseconds. The remaining half follow more diverse paths characterized by weaker electrostatic interactions and more than 10 times shorter transition path times. The chain flexibility and non-native interactions make diverse binding pathways possible, allowing disordered proteins to bind faster than folded proteins.

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Citations

Jan 14, 2021·Essays in Biochemistry·Pétur O Heidarsson, Ciro Cecconi
Dec 15, 2020·Journal of Molecular Biology·Nicolas PalopoliGustavo Parisi
Oct 23, 2020·Proceedings of the National Academy of Sciences of the United States of America·Rohit SatijaDmitrii E Makarov
Feb 23, 2021·The Journal of Physical Chemistry. B·Dmitrii E Makarov
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Mar 24, 2021·The Journal of Chemical Physics·Alexander M BerezhkovskiiDmitrii E Makarov
Mar 24, 2021·The Journal of Chemical Physics·Grace H Taumoefolau, Robert B Best
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Jun 7, 2021·Current Opinion in Chemical Biology·Marie Shimogawa, E James Petersson
Sep 11, 2021·Proceedings of the National Academy of Sciences of the United States of America·Felix WiggersHagen Hofmann

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