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Open AccessJournal ArticleDOI

Suppressing Brownian motion of individual biomolecules in solution

Adam E. Cohen, +1 more
- 21 Mar 2006 - 
- Vol. 103, Iss: 12, pp 4362-4365
TLDR
An anti-Brownian electrokinetic (ABEL) trap is used to trap individual protein molecules in free solution, under ambient conditions, without requiring any attachment to beads or surfaces.
Abstract
Single biomolecules in free solution have long been of interest for detailed study by optical methods, but Brownian motion prevents the observation of one single molecule for extended periods. We have used an anti-Brownian electrokinetic (ABEL) trap to trap individual protein molecules in free solution, under ambient conditions, without requiring any attachment to beads or surfaces. We also demonstrate trapping and manipulation of single virus particles, lipid vesicles, and fluorescent semiconductor nanocrystals.

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Citations
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Journal ArticleDOI

Single-molecule force spectroscopy: optical tweezers, magnetic tweezers and atomic force microscopy

TL;DR: These techniques are described and illustrated with examples highlighting current capabilities and limitations of single-molecule force spectroscopy.
Journal ArticleDOI

Protein folding studied by single-molecule FRET.

TL;DR: Single-molecule fluorescence studies are still in their infancy and have already produced novel and important information on current issues in protein folding that has been impossible or difficult to obtain from ensemble measurements.
Journal ArticleDOI

New directions in single-molecule imaging and analysis

TL;DR: Optical imaging and analysis of single molecules continue to unfold as powerful ways to study the individual behavior of biological systems, unobscured by ensemble averaging as mentioned in this paper, as evidenced by new meetings, journal special issues, and the large number of new investigators.
Journal ArticleDOI

Toward dynamic structural biology: Two decades of single-molecule Förster resonance energy transfer

TL;DR: The evolution of smFRET as a key tool for “dynamic structural biology” over the past 22 years is reviewed and the prospects for its use in applications such as biosensing, high-throughput screening, and molecular diagnostics are highlighted.
Journal ArticleDOI

Single-Molecule Studies of Protein Folding

TL;DR: It is concluded that, although there have been relatively few startling insights from single-molecule studies, the rapid progress that has been made suggests that these experiments have significant potential to advance the understanding of protein folding.
References
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Journal ArticleDOI

Observation of a single-beam gradient force optical trap for dielectric particles

TL;DR: Optical trapping of dielectric particles by a single-beam gradient force trap was demonstrated for the first reported time, confirming the concept of negative light pressure due to the gradient force.
Journal ArticleDOI

Optical Trapping and Manipulation of Viruses and Bacteria

Arthur Ashkin, +1 more
- 20 Mar 1987 - 
TL;DR: Trapping and manipulation of single live motile bacteria and Escherichia coli bacteria were demonstrated in a high-resolution microscope at powers of a few milliwatts.
Journal ArticleDOI

Single-Molecule Measurement of Protein Folding Kinetics

TL;DR: This combination of a microfabricated laminar-flow mixer to a confocal optical system enables time-resolved measurement of Förster resonance energy transfer after an abrupt change in solution conditions.
Journal ArticleDOI

Microfabricated arrays of femtoliter chambers allow single molecule enzymology.

TL;DR: A silicone device presenting a large array of micrometer-sized cavities is developed to tightly enclose volumes of solution, as low as femtoliters, over long periods of time and demonstrated the feasibility of the approach by measuring the activity of single molecules of β-galactosidase and horseradish peroxidase.
Journal ArticleDOI

Osmotic pressure inhibition of DNA ejection from phage

TL;DR: The authors' experiments monitor directly a dramatic decrease of the stress inside the unopened phage capsid upon addition of polyvalent cations to the host solution, in agreement with many recent theories of DNA interactions.
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