Single-Molecule Force Spectroscopy of Protein Folding
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Petrosyan, R., Narayan, A., & Woodside, M. T. (2021). Single-Molecule Force Spectroscopy of Protein Folding. JOURNAL OF MOLECULAR BIOLOGY, 433(20), 167207. https://doi-org.login.ezproxy.library.ualberta.ca/10.1016/j.jmb.2021.167207
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The use of force probes to induce unfolding and refolding of single molecules through the application of mechanical tension, known as single-molecule force spectroscopy (SMFS), has proven to be a powerful tool for studying the dynamics of protein folding. Here we provide an overview of what has been learned about protein folding using SMFS, from small, single-domain proteins to large, multi-domain proteins. We highlight the ability of SMFS to measure the energy landscapes underlying folding, to map complex pathways for native and non-native folding, to probe the mechanisms of chaperones that assist with native folding, to elucidate the effects of the ribosome on co-translational folding, and to monitor the folding of membrane proteins.
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http://purl.org/coar/resource_type/c_6501 http://purl.org/coar/version/c_b1a7d7d4d402bcce http://purl.org/coar/version/c_71e4c1898caa6e32
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en