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Force Spectroscopy
Force Spectroscopy
Biomolecule
Molecular Recognition
Nanometre
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Atomic force microscopy-based single-molecule-force spectroscopy is limited by low throughput. We introduce addressable DNA origami to study multiple target molecules. Six target DNAs that differed by only a single base-pair mismatch were clearly differentiated a rupture force of only 4 pN.
Force Spectroscopy
Base (topology)
Scanning Force Microscopy
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Force Spectroscopy
Folding (DSP implementation)
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ABSTRACT 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 scales. However, unavoidable calibration errors of AFM probes make it cumbersome to quantify modulation of mechanics. Here, we show that concurrent AFM force measurements enable relative mechanical characterization with an accuracy that is independent of calibration uncertainty, even when averaging data from multiple, independent experiments. Compared to traditional AFM, we estimate that concurrent strategies can measure differences in protein mechanical unfolding forces with a 6-fold improvement in accuracy and a 30-fold increase in throughput. Prompted by our results, we demonstrate widely applicable orthogonal fingerprinting strategies for concurrent single-molecule nanomechanical profiling of proteins.
Force Spectroscopy
Profiling (computer programming)
Characterization
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Abstract 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 scales. However, unavoidable calibration errors of AFM probes make it cumbersome to quantify modulation of mechanics. Here, we show that concurrent AFM force measurements enable relative mechanical characterization with an accuracy that is independent of calibration uncertainty, even when averaging data from multiple, independent experiments. Compared to traditional AFM, we estimate that concurrent strategies can measure differences in protein mechanical unfolding forces with a 6-fold improvement in accuracy or a 30-fold increase in throughput. Prompted by our results, we demonstrate widely applicable orthogonal fingerprinting strategies for concurrent single-molecule nanomechanical profiling of proteins.
Force Spectroscopy
Profiling (computer programming)
Characterization
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This review briefly introduces the principles of atomic force microscopy (AFM) applied to protein samples. AFM provides three-dimensional surface images of the proteins with high resolution. The advantage of AFM for protein studies is that AFM can visualize directly the molecule under physiological conditions without previous treatment. AFM operated in the force-spectroscopy mode is now a widespread technique, often used to investigate ligand-receptor interactions with the goal of measuring forces at the individual molecule level. Keywords: afm, force spectroscopy, proteins adsorption, proteins structure, probe, sample interaction, afm imaging
Force Spectroscopy
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Atomic force microscopy (AFM) has provided a new and powerful tool in the investigation of single atoms, molecules and their interactions. Single molecule force spectroscopy (SMFS) is a force measurement based on AFM. A review is given on the development of single molecule polymer force studies by AFM-based SMFS in recent years.
Force Spectroscopy
Scanning Force Microscopy
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Force Spectroscopy
Scanning Force Microscopy
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Atomic force microscopy (AFM)-based single molecule force spectroscopy (SMFS) is one of the most useful methods in the investigation of intra- or intermolecular interactions. To simplify the sample system and the data analysis, real biological and material systems have usually been simplified, and the target molecule of interest is normally extracted and bridged between the AFM tip and substrate for study, which is an effective way of understanding the real systems. With the development of technology (including the improvement of sample immobilization method), it is possible now to directly investigate molecular interactions in living system and real materials. The information obtained will be more useful for the better control of relevant biological processes and the design of high performance polymer materials. In this paper, recent progresses in AFM-SMFS study of molecular interactions in living cells and polymer materials are reviewed.
Force Spectroscopy
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The force acting between molecules and substrates is crucial for the manipulation process. Atomic force microscopy (AFM) is not only a versatile tool for imaging in biological research, but also a versatile one for the manipulation of biological molecules. Because of the high mechanical resolution of AFM, it is preferred for the study of the interaction of mechanics in biological systems. This work is focused on the using of the Single-molecule force spectroscopy based on AFM (AFM-SMFS) method in the process of DNA manipulation. It explored the manipulation methods based on AFM, and then introduced one of the modification methods of the DNA molecules and the AFM cantilever. Compared with the different statements of the AFM cantilever by AFM-SMFS, analyzed the adhesion force between the molecules and the substrates.
Force Spectroscopy
Chemical force microscopy
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