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Editor's evaluation: Unfolding and identification of membrane proteins in situ
Single-molecule force spectroscopy (SMFS) uses the cantilever tip of an atomic force microscope (AFM) to apply a force able to unfold a single protein. The obtained force-distance curve encodes the unfolding pathway, and from its analysis it is possible to characterize the folded domains. SMFS has been mostly used to study the unfolding of purified proteins, in solution or reconstituted in a lipid bilayer. Here, we describe a pipeline for analyzing membrane proteins based on SMFS, whichdoi:10.7554/elife.77427.sa0 fatcat:5s7bo2bflvf5foqsdxchtcjuxu