High-speed Afm
High-speed Afm - Related Videos
08:21
Quantitative Hardness Measurement by Instrumented AFM-indentation
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Cited by 6 •
2016
This experimental protocol describes how atomic force microscopy can be used to measure hardness at the true nanometer scale and to detect single atomistic plasticity events.
09:47
AFM and Microrheology in the Zebrafish Embryo Yolk Cell
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Cited by 3 •
2017
The lack of tools to measure material properties and tensional parameters in vivo prevents validating their roles during development. We employed atomic force microscopy (AFM) and nanoparticle-tracking to quantify mechanical features on the intact zebrafish embryo yolk cell during epiboly. These methods are reliable and widely applicable avoiding intrusive interventions.
04:56
High-Speed Time-Lapse Atomic Force Microscopy to Capture Nucleosome Dynamics
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2025
In this video, we demonstrate high-speed time-lapse atomic force microscopy, AFM, imaging techniques to study the dynamics of nucleosome complexes. As the AFM tip scans across the surface of the nucleosome, it detects alterations in the nucleosome height and records the DNA unwrapping over time.
08:29
Au-Interaction of Slp1 Polymers and Monolayer from Lysinibacillus sphaericus JG-B53 - QCM-D, ICP-MS and AFM as Tools for Biomolecule-metal Studies
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Cited by 12 •
2016
To obtain basic information on the sorption and recycling of gold from aqueous systems the interaction of Au(III) and Au(0) nanoparticles on S-layer proteins were investigated. The sorption of protein polymers was investigated by ICP-MS and that of proteinaceous monolayers by QCM-D. Subsequent AFM enables the imaging of the nanostructures.
01:27
Distribution of Molecular Speeds
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2023
The motion of molecules in a gas is random in magnitude and direction for individual molecules, but a gas of many molecules has a predictable distribution of molecular speeds. This predictable distribution of molecular speeds is known as the Maxwell-Boltzmann distribution. The distribution of molecular speeds in liquids is comparable to that of gases but not identical and can help to understand the phenomenon of the boiling and vapor pressure of a liquid. Consider that a molecule requires a...
FAQs
During scanning, the probe encounters force changes at the sample surface, which alter the cantilever’s motion. The system detects those changes and uses feedback to adjust the tip-to-sample distance, preserving a controlled interaction while the image is acquired. This closed-loop response is central to tracking surface features as they change rather than merely recording a static shape.
Probe sharpness and cantilever motion work together to resolve nanoscale surface behavior. The sharp probe scans the sample, while force-dependent changes in the oscillating cantilever supply the signal used for distance control. Maintaining this controlled interaction helps the instrument follow changing molecular surfaces, supporting observations of motion and structural transitions rather than relying only on a final image.
Compared with conventional AFM, High-speed AFM is intended to capture surface dynamics in near real time. That difference matters when a biological event changes during observation, because a slower measurement may miss the transition or sequence of states. The technique therefore adds a temporal view to nanoscale imaging, allowing structure to be considered together with motion and kinetics.
A typical measurement begins with positioning a biological sample for scanning, bringing the sharp probe into controlled interaction with its surface, and monitoring the rapidly oscillating cantilever. Force-dependent motion is detected during the scan, while feedback continually adjusts the tip-to-sample distance. The resulting measurement records nanoscale surface changes over time rather than treating the sample as stationary.
Liquid conditions are important because High-speed AFM can observe biological molecules in that setting while they undergo dynamic processes. This makes the approach suitable for examining conformational changes, assembly, transport, and enzymatic activity. When the measurement is performed under liquid, researchers can relate observed surface dynamics to function without adding fluorescent labels.
The method is especially useful when the research question concerns how a biological molecule changes, assembles, moves, or performs an enzymatic function. Its measurements can connect molecular structure with motion and kinetics, providing direct insight into the timing and progression of observed surface events. Because imaging does not require fluorescent labels, High-speed AFM offers a complementary way to study these processes.