title: May the force be with you: unfolding lipid-protein interactions by single-molecule force spectroscopy.
abstract: In this issue of Structure, Serdiuk et al. report the use of single-molecule force microscopy to establish a role for phosphatidylethanolamine in promoting the native fold of lactose permease, thereby preventing it from populating a functionally defective, nonnative conformation (Serdiuk et al., 2015).
authors: Department of Biochemistry and Molecular Biology, University of Texas Medical School-Houston, Houston, TX 77030, USA. Electronic address: william.dowhan@uth.tmc.edu.
authors: William
authors: W
authors: Dowhan
authors: Department of Biochemistry and Molecular Biology, University of Texas Medical School-Houston, Houston, TX 77030, USA.
authors: Heidi
authors: H
authors: Vitrac
authors: Department of Biochemistry and Molecular Biology, University of Texas Medical School-Houston, Houston, TX 77030, USA.
authors: Mikhail
authors: M
authors: Bogdanov
mesh_terms: D029968:Escherichia coli Proteins / Q000737:chemistry*; D008563:Membrane Lipids / Q000737:chemistry*; D056004:Molecular Dynamics Simulation; D009004:Monosaccharide Transport Proteins / Q000737:chemistry*; D027981:Symporters / Q000737:chemistry*
chemical_list: D029968:Escherichia coli Proteins; D008563:Membrane Lipids; D009004:Monosaccharide Transport Proteins; D027981:Symporters