The Experts below are selected from a list of 87456 Experts worldwide ranked by ideXlab platform
Attila Nagy - One of the best experts on this subject based on the ideXlab platform.
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Single-molecule Force Spectroscopy: optical tweezers, magnetic tweezers and atomic Force microscopy
Nature Methods, 2008Co-Authors: Keir C. Neuman, Attila NagyAbstract:Single-molecule Force Spectroscopy has emerged as a powerful tool to investigate the Forces and motions associated with biological molecules and enzymatic activity. The most common Force Spectroscopy techniques are optical tweezers, magnetic tweezers and atomic Force microscopy. Here we describe these techniques and illustrate them with examples highlighting current capabilities and limitations.
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single molecule Force Spectroscopy optical tweezers magnetic tweezers and atomic Force microscopy
Nature Methods, 2008Co-Authors: Keir C. Neuman, Attila NagyAbstract:Single-molecule Force Spectroscopy: optical tweezers, magnetic tweezers and atomic Force microscopy
Keir C. Neuman - One of the best experts on this subject based on the ideXlab platform.
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SnapShot: Force Spectroscopy and Single-Molecule Manipulation
Cell, 2013Co-Authors: Yeonee Seol, Keir C. NeumanAbstract:The deflection of a cantilever is measured using a laser beam and position-sensing detector to obtain Force and displacement for both imaging and Force Spectroscopy. In Force Spectroscopy, the cantilever is attached to one end of the protein or DNA sample while the other end is immobilized on the surface. The Force and position of the tip are measured as the surface is moved away from the tip, providing the Force-extension curve of the sample.High spatial resolution (0.5–1 nm); temporal resolution (>1 KHz); high Force range (10–10
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Single-molecule Force Spectroscopy: optical tweezers, magnetic tweezers and atomic Force microscopy
Nature Methods, 2008Co-Authors: Keir C. Neuman, Attila NagyAbstract:Single-molecule Force Spectroscopy has emerged as a powerful tool to investigate the Forces and motions associated with biological molecules and enzymatic activity. The most common Force Spectroscopy techniques are optical tweezers, magnetic tweezers and atomic Force microscopy. Here we describe these techniques and illustrate them with examples highlighting current capabilities and limitations.
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single molecule Force Spectroscopy optical tweezers magnetic tweezers and atomic Force microscopy
Nature Methods, 2008Co-Authors: Keir C. Neuman, Attila NagyAbstract:Single-molecule Force Spectroscopy: optical tweezers, magnetic tweezers and atomic Force microscopy
Andre Marziali - One of the best experts on this subject based on the ideXlab platform.
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single molecule bonds characterized by solid state nanopore Force Spectroscopy
ACS Nano, 2009Co-Authors: Vincent Tabardcossa, Matthew Wiggin, Dhruti Trivedi, Nahid N Jetha, Jason R Dwyer, Andre MarzialiAbstract:Weak molecular interactions drive processes at the core of living systems, such as enzyme−substrate interactions, receptor−ligand binding, and nucleic acid replication. Single-molecule Force Spectroscopy is a remarkable tool for revealing molecular scale energy landscapes of noncovalent bonds, by exerting a mechanical Force directly on an individual molecular complex and tracking its survival as a function of time and applied Force. In principle, Force Spectroscopy methods can also be used for highly specific molecular recognition assays, by directly characterizing the strength of bonds between probe and target molecules. However, complexity and low throughput of conventional Force Spectroscopy techniques render such biosensing applications impractical. Here we demonstrate a straightforward single-molecule approach, suitable for both biophysical studies and molecular recognition assays, in which a ∼3 nm silicon nitride nanopore is used to determine the bond lifetime spectrum of the biotin−neutravidin comp...
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Nanopore Force Spectroscopy on DNA duplexes.
Methods in molecular biology (Clifton N.J.), 2009Co-Authors: Nahid N Jetha, Matthew Wiggin, Andre MarzialiAbstract:Force Spectroscopy can be applied using nanopores to study charged molecules such as nucleic acids. This technique can be used to study the binding energy of a DNA duplex by threading an anchored single-stranded DNA (ssDNA) probe molecule through a nanopore (having a diameter large enough to accommodate only a single strand) and allowing target DNA on the backside of the pore to hybridize to the probe. Electric potential can be used to apply a Force to the charged ssDNA in a direction tending to translocate the duplex through the pore. If the pore is only large enough to accept ssDNA, the duplex must dissociate for the probe to escape the pore. The dissociation time of the duplex can therefore be measured under applied Force, and (provided that enough dissociation events have been recorded) a characteristic time scale for dissociation can be determined. In this chapter, we present a detailed protocol for performing nanopore Force Spectroscopy on DNA duplexes using one or more alpha-hemolysin nanopores. We present the details of the measurement of the duplex survival probability under Force, and show that dissociation time scales for duplexes that are perfectly complimentary differ by greater than approximately two orders of magnitude from those containing a single sequence mismatch, offering opportunities for sequence detection.
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Multi-Nanopore Force Spectroscopy for DNA Analysis
Biophysical journal, 2006Co-Authors: Carolina Tropini, Andre MarzialiAbstract:The need for low-cost DNA sequence detection in clinical applications is driving development of new technologies. We demonstrate a method for detection of mutations in a DNA sequence purely by electronic means, and without need for fluorescent labeling. Our method uses an array of nanopores to perform synchronized single-molecule Force Spectroscopy measurements over many molecules in parallel, yielding detailed information on the kinetics of hundreds of molecule dissociations in a single measurement.
Daniel J. Müller - One of the best experts on this subject based on the ideXlab platform.
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Single-Molecule Force Spectroscopy of Transmembrane β-Barrel Proteins.
Annual review of analytical chemistry (Palo Alto Calif.), 2018Co-Authors: Johannes Thoma, K. Tanuj Sapra, Daniel J. MüllerAbstract:Single-molecule Force Spectroscopy (SMFS) has been widely applied to study the mechanical unfolding and folding of transmembrane proteins. Here, we review the recent progress in characterizing bact...
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Quantifying cellular adhesion to extracellular matrix components by single-cell Force Spectroscopy
Nature Protocols, 2010Co-Authors: Jens Friedrichs, Jonne Helenius, Daniel J. MüllerAbstract:Quantifying cellular adhesion to extracellular matrix components by single-cell Force Spectroscopy
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single cell Force Spectroscopy
Journal of Cell Science, 2008Co-Authors: Jonne Helenius, Hermann E. Gaub, Carlphilipp Heisenberg, Daniel J. MüllerAbstract:The controlled adhesion of cells to each other and to the extracellular matrix is crucial for tissue development and maintenance. Numerous assays have been developed to quantify cell adhesion. Among these, the use of atomic Force microscopy (AFM) for single-cell Force Spectroscopy (SCFS) has recently been established. This assay permits the adhesion of living cells to be studied in near-physiological conditions. This implementation of AFM allows unrivaled spatial and temporal control of cells, as well as highly quantitative Force actuation and Force measurement that is sufficiently sensitive to characterize the interaction of single molecules. Therefore, not only overall cell adhesion but also the properties of single adhesion-receptor–ligand interactions can be studied. Here we describe current implementations and applications of SCFS, as well as potential pitfalls, and outline how developments will provide insight into the Forces, energetics and kinetics of celladhesion processes.
Lawrence A. Bottomley - One of the best experts on this subject based on the ideXlab platform.
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Plastic tip arrays for Force Spectroscopy.
Analytical Chemistry, 2004Co-Authors: Peter T. Lillehei, Mark A. Poggi, Brian J. Polk, And J. Anthony Smith, Lawrence A. BottomleyAbstract:The mechanical stability and viability of molecules investigated with the atomic Force microscope (AFM) continue to be limiting factors in the duration of Force Spectroscopy measurements. In an eff...
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Plastic tip arrays for Force Spectroscopy.
Analytical chemistry, 2004Co-Authors: Peter T. Lillehei, Mark A. Poggi, Brian J. Polk, And J. Anthony Smith, Lawrence A. BottomleyAbstract:The mechanical stability and viability of molecules investigated with the atomic Force microscope (AFM) continue to be limiting factors in the duration of Force Spectroscopy measurements. In an effort to circumvent this problem, we have fabricated an all-plastic array of over 30 000 tips with dimensions similar to common AFM probes using silicon micromolding techniques. This approach enables rapid fabrication of tip arrays with improved properties, as compared to tip arrays made entirely of silicon.