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Single-molecule techniques have been used successfully to visualize real-time enzymatic activities, revealing transient complex properties and heterogeneity of various biological events. Especially, conventional force spectroscopy including optical tweezers and magnetic tweezers has been widely used to monitor change in DNA length by enzymes with high spatiotemporal resolutions of ∼nanometers and ∼milliseconds. However, DNA metabolism results from coordination of a number of components during th

Single-molecule force spectroscopy often refers to the measurement of the enzymatic activities coupled to the mechanical properties of biomolecules. We apply a simple dark-field microscope to a single-molecule flow-stretching method that quantitatively measures thermal fluctuations of the micron bead linked to DNA under a hydrodynamic force. Using various lengths of DNA attached to the bead, we measured the external force exerted on DNA immobilized on the surface and quantitatively showed the an