Journal ArticleDOI
Sensing specific molecular interactions with the atomic force microscope
Ernst-Ludwig Florin,Matthias Rief,Horst Lehmann,Markus Ludwig,C. Dornmair,Vincent T. Moy,Hermann E. Gaub +6 more
TLDR
Here, different techniques that allow for the in situ measurement of the absolute value of the spring constant of the cantilevers are compared.About:
This article is published in Biosensors and Bioelectronics.The article was published on 1995-01-01. It has received 469 citations till now. The article focuses on the topics: Magnetic force microscope.read more
Citations
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Single Molecule Force Spectroscopy on Polysaccharides by Atomic Force Microscopy
TL;DR: Dextran filaments linked to a gold surface were probed with the atomic force microscope tip by vertical stretching and the conformational change was found to be reversible and was corroborated by molecular dynamics calculations.
Journal ArticleDOI
Mechanical and Chemical Unfolding of a Single Protein: A Comparison
Mariano Carrión-Vázquez,Andres F. Oberhauser,Susan B. Fowler,Piotr E. Marszalek,Sheldon E. Broedel,Jane Clarke,Julio M. Fernandez +6 more
TL;DR: The results indicate that mechanical unfolding of a single protein by AFM does indeed reflect the same event that is observed in traditional unfolding experiments, and the way is now open for the extensive use of AFM to measure folding reactions at the single-molecule level.
Journal ArticleDOI
The molecular elasticity of the extracellular matrix protein tenascin
TL;DR: It is suggested that the extensibility of the modular fibronectin type III region may be important in allowing tenascin–ligand bonds to persist over long extensions, and of widespread use in extracellular proteins containing such domain.
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A biosensor based on magnetoresistance technology.
David R. Baselt,Gil U. Lee,Mohan Natesan,Steven W. Metzger,Paul E. Sheehan,Richard J. Colton +5 more
TL;DR: A biosensor that will measure, at the level of single molecules, the forces that bind DNA-DNA, antibody-antigen, or ligand-receptor pairs together, and the potential to directly gauge intermolecular interaction strengths suggests drug discovery applications.
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Mechanical unfolding intermediates in titin modules.
Piotr E. Marszalek,Hui Lu,Hongbin Li,Mariano Carrión-Vázquez,Andres F. Oberhauser,Klaus Schulten,Julio M. Fernandez +6 more
TL;DR: This work reports the elongation of single proteins to have multiple copies of single immunoglobulin domains of human cardiac titin using the atomic force microscope, and finds an abrupt extension of each domain by ∼7 Å before the first unfolding event, likely to be an important previously unrecognized component of titin elasticity.
References
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Atomic force microscope
TL;DR: The atomic force microscope as mentioned in this paper is a combination of the principles of the scanning tunneling microscope and the stylus profilometer, which was proposed as a method to measure forces as small as 10-18 N. As one application for this concept, they introduce a new type of microscope capable of investigating surfaces of insulators on an atomic scale.
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Calibration of atomic‐force microscope tips
TL;DR: In this article, the authors describe a simple, nondestructive procedure for measuring the force constant, resonant frequency, and quality factor of an AFM cantilever spring and the effective radius of curvature of an AU tip.
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Adhesion forces between individual ligand-receptor pairs.
TL;DR: Under conditions that allowed only a limited number of molecular pairs to interact, the force required to separate tip and bead was found to be quantized in integer multiples of 160 +/- 20 piconewtons for biotin and 85 +/- 15 piconewstons for iminobiotin.
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Direct observation of kinesin stepping by optical trapping interferometry
TL;DR: It is found that kinesin moves with 8-nm steps, similar to biological motors that move with regular steps.