Journal
COMMUNICATIONS CHEMISTRY
Volume 1, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/s42004-018-0060-9
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Funding
- European Research Council [ERC-2012-ADG-323059]
- Spanish Ministry of Economy and Competitiveness [CTQ2015-65320-R, RYC-2016- 19590, BIO2016-77390-R]
- I-CORE Program of the Planning and Budgeting Committee
- Israel Science Foundation [152/11]
- National Institute of Diabetes and Digestive and Kidney Diseases of the National Institutes of Health
- W.M. Keck Foundation
- CREST Center for Cellular and Biomolecular Machines [NSF-CREST-1547848]
- NSF [MCB-1616759]
- European Commission CIG Marie Curie Reintegration program FP7-PEOPLE-2014
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Ultrafast folding proteins have limited cooperativity and thus are excellent models to resolve, via single-molecule experiments, the fleeting molecular events that proteins undergo during folding. Here we report single-molecule atomic force microscopy experiments on gpW, a protein that, in bulk, folds in a few microseconds over a marginal folding barrier (similar to 1 k(B)T). Applying pulling forces of only 5 pN, we maintain gpW in quasi-equilibrium near its mechanical unfolding midpoint and detect how it interconverts stochastically between the folded and an extended state. The interconversion pattern is distinctly binary, indicating that, under an external force, gpW (un) folds over a significant free-energy barrier. Using molecular simulations and a theoretical model we rationalize how force induces such barrier in an otherwise downhill free-energy surface. Force-induced folding barriers are likely a general occurrence for ultrafast folding biomolecules studied with single-molecule force spectroscopy.
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