Unfolding pathways of individual bacteriorhodopsins.

By F. Oesterhelt, D. Oesterhelt, Matthias Pfeiffer, Andreas Engel, H. Gaub, Daniel J. Müller. Science, 2000

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Single-molecule force spectroscopy: optical tweezers, magnetic tweezers and atomic force microscopy (2008, methodology): “In one example, purple membrane patches were imaged with the atomic force microscope to find the location of an individual bacteriorhodopsin molecule, which was then extracted with the same AFM tip so the unbinding forces and force spectrum of removal could be measure”
Biomedical Nanomagnetics: A Spin Through Possibilities in Imaging, Diagnostics, and Therapy (2010, neutral): “Note that the Langevin function is also used to describe the force-displacement behavior of proteins and the protein unfolding dynamics [33] of importance in biology.”
Biomolecules under mechanical force (2010, neutral): “065 87 350 [375,376] T4-Lysozyme 1B6I 162 α/β 35.”
Stability of Bacteriorhodopsin α-Helices and Loops Analyzed by Single-Molecule Force Spectroscopy (2002, background): “In a previous study (Oesterhelt et al., 2000), we already had assigned the main peaks to different processes: the peaks below 20 nm include unfolding of helices G and F.”