Force spectroscopy based on temperature controlled atomic force microscope head using piezoresistive cantilevers

2005 ◽  
Vol 76 (4) ◽  
pp. 043701 ◽  
Author(s):  
I. Muševič ◽  
K. Kočevar ◽  
U. Kržič ◽  
G. Carbone
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

2019 ◽  
Vol 86 (s1) ◽  
pp. 12-16
Author(s):  
Janik Schaude ◽  
Julius Albrecht ◽  
Ute Klöpzig ◽  
Andreas C. Gröschl ◽  
Tino Hausotte

AbstractThis article presents a new tilting atomic force microscope (AFM) with an adjustable probe direction and piezoresistive cantilever operated in tapping-mode. The AFM is based on two rotational axes, which enable the adjustment of the probe direction to cover a complete hemisphere. The whole setup is integrated into a nano measuring machine (NMM-1) and the metrological traceability of the piezoresistive cantilever is warranted by in situ calibration on the NMM-1. To demonstrate the capabilities of the tilting AFM, measurements were conducted on a step height standard.


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.


2019 ◽  
Vol 11 (37) ◽  
pp. 4709-4718 ◽  
Author(s):  
Tal Duanis-Assaf ◽  
Yair Razvag ◽  
Meital Reches

Single molecule force spectroscopy (SMFS) using an atomic force microscope is a common method in the study of ligand–receptor interactions, adhesion events and protein folding. ForSDAT is a platform for automated data analysis of SMFS data.


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