Single-molecule force spectroscopy with the atomic force microscope provides molecular
level insights into protein function, allowing researchers to reconstruct energy landscapes …

Complete understanding of the role of mechanical forces in biological processes requires
knowledge of the mechanical properties of individual proteins and living cells. Moreover, the …

Multiple gram-negative bacteria encode type III secretion systems (T3SS) that allow them to
inject effector proteins directly into host cells to facilitate colonization. To be secreted …

Single-molecule force spectroscopy is a powerful tool for studying protein folding. Over the
last decade, a key question has emerged: how are changes in intrinsic biomolecular …

Ligand-induced conformational changes are critical to the function of many membrane
proteins and arise from numerous intramolecular interactions. In the photocycle of the model …

Atomic force microscopy (AFM)-based single-molecule force spectroscopy (SMFS) is a
powerful yet accessible means to characterize the unfolding/refolding dynamics of individual …

We quantified the equilibrium (un) folding free energy Δ G 0 of an eight-amino-acid region
starting from the fully folded state of the model membrane-protein bacteriorhodopsin using …

Precise quantification of the energetics and interactions that stabilize membrane proteins in
a lipid bilayer is a long-sought goal. Toward this end, atomic force microscopy has been …

Single amino acid mutations provide quantitative insight into the energetics that underlie the
dynamics and folding of membrane proteins. Chemical denaturation is the most widely used …

Force-spectroscopy by atomic force microscopy (AFM) is the technique of choice to measure
mechanical properties of molecules, cells, tissues and materials at the nano and micro …