Force Spectroscopy of Single Protein Molecules Using an Atomic Force Microscope

Author(s):  
Zackary N. Scholl ◽  
Qing Li ◽  
Eric Josephs ◽  
Dimitra Apostolidou ◽  
Piotr E. Marszalek
2007 ◽  
Vol 35 (6) ◽  
pp. 1564-1568 ◽  
Author(s):  
D.J. Brockwell

The mechanical strength of single protein molecules can be investigated by using the atomic force microscope. By applying this technique to a wide range of proteins, it appears that the type of secondary structure and its orientation relative to the extension points are important determinants of mechanical strength. Unlike chemical denaturants, force acts locally and the mechanical strength of a protein may thus appear to be mechanically weak or strong by simply varying the region of the landscape through which the protein is unfolded. Similarly, the effect of ligand binding on the mechanical resistance of a protein may also depend on the relative locations of the binding site and force application. Mechanical deformation may thus facilitate the degradation or remodelling of thermodynamically stable proteins and their complexes in vivo.


2011 ◽  
Vol 414 (1) ◽  
pp. 1-6 ◽  
Author(s):  
Hans A. Heus ◽  
Elias M. Puchner ◽  
Aafke J. van Vugt-Jonker ◽  
Julia L. Zimmermann ◽  
Hermann E. Gaub

Leonardo ◽  
2009 ◽  
Vol 42 (3) ◽  
pp. 186-192 ◽  
Author(s):  
Paul Thomas

The Midas project investigates the trans-mediational space between skin and gold. Research for the project was conducted through the analysis of data recorded with an Atomic Force Microscope (AFM). The AFM, in its force spectroscopy mode, gathers data by picking up the surface vibrations as the cantilever touches the cell. The Midas project culminated in an installation that included data projection and audio work utilizing subsonic speakers to make the data from the atomic vibrations audible and palpable.


2015 ◽  
Vol 6 (31) ◽  
pp. 5740-5751 ◽  
Author(s):  
Cesar Rodriguez-Emmenegger ◽  
Sébastien Janel ◽  
Andres de los Santos Pereira ◽  
Michael Bruns ◽  
Frank Lafont

The adhesion forces between a single bacterial cell and different polymer brushes were measured directly with an atomic force microscope and correlated with their resistance to fouling.


1999 ◽  
Vol 70 (11) ◽  
pp. 4300-4303 ◽  
Author(s):  
M. B. Viani ◽  
T. E. Schäffer ◽  
G. T. Paloczi ◽  
L. I. Pietrasanta ◽  
B. L. Smith ◽  
...  

1997 ◽  
Vol 5 (7) ◽  
pp. 3-7
Author(s):  
Stephen W. Carmichael

A recent article by Matthias Rief, Filipp Oesterhelt. Berthold Heymann, and Hermann Gaub concluded with this sentence: "Single molecule force spectroscopy by AFM has proven to be a powerful addition to the nanoscopic piconewton toolbox," Everything about that conclusion is tiny. Clearly, the atomic force microscope (AFM) has given us a tool to examine structure at or near the atomic level. Earlier work from Gaub's laboratory, reviewed in this column, demonstrated that the AFM could directly measure the binding force between single molecules of biotin and avidin. This established that the AFM could be used as a tool to measure forces, not just observe structure. Their most recent experiments has added to this tiny toolbox.


2019 ◽  
Author(s):  
◽  
Anna Elizabeth Pittman

In my projects, I used the Atomic Force Microscope (AFM) to image the effects of pore-forming peptides and I used the Focused Ion Beam (FIB) to modify AFM cantilevers to increase the precision of force spectroscopy measurements. ... Another way to investigate peptide-lipid interactions is to perform force spectroscopy experiments using the AFM. In order to lower drift and increase force precision, I used a FIB to modify commercially available AFM cantilevers. By reducing the cross sectional area of the cantilever, the hydrodynamic drag was reduced, thus increasing the force precision. Removing most of the gold coating on the cantilever increased the temporal stability. These modified cantilevers have already been put to use in the lab to measure peptide-lipid interactions.


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