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Significance Atomic force microscopy is widely used to unravel proteins. We modulated the protein's folding rate using pH to address concerns that the measured dynamics of such proteins are dominated by the AFM assay. Despite the reconstructed landscape being dominated by the assay, Kinetic results showed changes in free-energy landscape parameters with pH assay.
Source link: https://doi.org/10.1073/pnas.2015728118
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