Graphite Particle Adhesion to Hastelloy X: Measurements of the Adhesive Force with an Atomic Force Microscope

2014 ◽  
Vol 186 (1) ◽  
pp. 45-59 ◽  
Author(s):  
Naphtali M. Mokgalapa ◽  
Tushar K. Ghosh ◽  
Sudarshan K. Loyalka
Keyword(s):  
Atomic Force Microscope ◽  
Graphite Particle ◽  
Adhesive Force ◽  
Particle Adhesion ◽  
Hastelloy X ◽  
Atomic Force

scholarly journals The influence of epitope availability on atomic-force microscope studies of antigen–antibody interactions

1999 ◽  
Vol 341 (1) ◽  
pp. 173-178 ◽  
Author(s):  
Stephanie ALLEN ◽  
John DAVIES ◽  
Martyn C. DAVIES ◽  
Adrian C. DAWKES ◽  
Clive J. ROBERTS ◽  
...  
Keyword(s):  
Atomic Force Microscope ◽  
Adhesive Force ◽  
Biological Molecules ◽  
Binding Studies ◽  
Periodic Force ◽  
Atomic Force ◽  
Binding Data ◽  
Single Antigen ◽  
Antigen Antibody ◽  
Antibody Interactions

The ability of the atomic-force microscope (AFM) to detect interaction forces between individual biological molecules has recently been demonstrated. In this study, force measurements have been obtained between AFM probes functionalized with the β-subunit of human chorionic gonadotrophin (βhCG) and surfaces functionalized with anti-βhCG antibody. A comparison of the obtained results with previous anti-ferritin antibody-binding data identifies differences when the antigen molecule expresses only a single epitope (βhCG), rather than multiple epitopes (ferritin), for the monoclonal antibodies employed. Specifically, the probability of observing probe-sample adhesion is found to be higher when the antigen expresses multiple epitopes. However, the periodic force observed in the adhesive-force distribution, due to the rupture of single antigen-antibody interactions, is found to be larger and more clearly observed for the mono-epitopic system. Hence, these findings indicate the potential of the AFM to distinguish between multivalent and monovalent antibody-antigen interactions, and demonstrate the influence of the number of expressed epitopes upon such binding studies.

Adhesive Force Reduction and Molecular Aggregation on Lubricin-Coated Contacts

2005 ◽  
Author(s):  
J. R. Torres ◽  
G. D. Jay ◽  
M. L. Warman ◽  
K. S. Kim
Keyword(s):  
Atomic Force Microscope ◽  
Hydrophobic Surface ◽  
Adhesive Force ◽  
Threshold Concentration ◽  
Molecular Aggregation ◽  
Uniform Coating ◽  
Atomic Force ◽  
Dry Conditions ◽  
Force Reduction

The atomic force microscope (AFM) was employed in dry conditions in order to test the surface modifying ability of lubricin. The present work shows that lubricin forms independent aggregates, which coalesce once a threshold concentration is reached providing uniform coating of a hydrophobic surface.

scholarly journals Changes in Nanoscaled Mechanical and Rheological Properties of Asphalt Binders Caused by Aging

2015 ◽  
Vol 2015 ◽  
pp. 1-6 ◽  
Author(s):  
Ben Liu ◽  
Junan Shen ◽  
Xuyan Song
Keyword(s):  
Thin Film ◽  
Atomic Force Microscope ◽  
Rheological Properties ◽  
Asphalt Binder ◽  
Adhesive Force ◽  
Asphalt Binders ◽  
Dynamic Shear ◽  
Short Term ◽  
Atomic Force ◽  
Aged Asphalt

Aging of an asphalt binder causes the changes in the microstructure and, consequently, in the nanomechanical and rheological properties of the aged asphalt binder. Short-term aging on asphalt binders was simulated using rotating thin film oven (RTFO). These changes in the microstructure and nanomechanical and rheological properties were measured using atomic force microscope (AFM) and dynamic shear rheometer (DSR). The results indicated that (1) the adhesive force of the asphalt binder from AFM tests was increased after RTFO aging; (2)G*of the asphalt binder from DSR tests increased after RTFO aging; (3) the results from AFM were consistent with those from DSR, explaining the mechanism of the changes of rheological properties.

Adhesive force distribution on microstructures investigated by an atomic force microscope

1994 ◽  
Vol 44 (2) ◽  
pp. 153-158 ◽  
Author(s):  
Akihiro Torii ◽  
Minoru Sasaki ◽  
Kazuhiro Hane ◽  
Shigeru Okuma
Keyword(s):  
Atomic Force Microscope ◽  
Adhesive Force ◽  
Force Distribution ◽  
Atomic Force

Characterization of photosystem II with the atomic-force microscope

1992 ◽  
Vol 50 (2) ◽  
pp. 1146-1147
Author(s):  
Kathleen M. Marr ◽  
Mary K. Lyon
Keyword(s):  
Photosystem Ii ◽  
Atomic Force Microscope ◽  
Three Dimensional ◽  
Biologically Active ◽  
Atomic Force ◽  
Freeze Etching ◽  
Image Averaging ◽  
Oxygen Evolving ◽  
Averaging Techniques

Photosystem II (PSII) is different from all other reaction centers in that it splits water to evolve oxygen and hydrogen ions. This unique ability to evolve oxygen is partly due to three oxygen evolving polypeptides (OEPs) associated with the PSII complex. Freeze etching on grana derived insideout membranes revealed that the OEPs contribute to the observed tetrameric nature of the PSIl particle; when the OEPs are removed, a distinct dimer emerges. Thus, the surface of the PSII complex changes dramatically upon removal of these polypeptides. The atomic force microscope (AFM) is ideal for examining surface topography. The instrument provides a topographical view of individual PSII complexes, giving relatively high resolution three-dimensional information without image averaging techniques. In addition, the use of a fluid cell allows a biologically active sample to be maintained under fully hydrated and physiologically buffered conditions. The OEPs associated with PSII may be sequentially removed, thereby changing the surface of the complex by one polypeptide at a time.

Imaging polymers, proteins and dna in aqueous solutions with the atomic force microscope

1989 ◽  
Vol 47 ◽  
pp. 32-33
Author(s):  
S.A.C. Gould ◽  
B. Drake ◽  
C.B. Prater ◽  
A.L. Weisenhorn ◽  
S.M. Lindsay ◽  
...  
Keyword(s):  
Amino Acids ◽  
Dna Sequencing ◽  
Aqueous Solutions ◽  
Atomic Force Microscope ◽  
Piezoelectric Crystal ◽  
Atomic Force ◽  
Structure Of Molecules ◽  
Optical Lever

The atomic force microscope (AFM) is an instrument that can be used to image many samples of interest in biology and medicine. Images of polymerized amino acids, polyalanine and polyphenylalanine demonstrate the potential of the AFM for revealing the structure of molecules. Images of the protein fibrinogen which agree with TEM images demonstrate that the AFM can provide topographical data on larger molecules. Finally, images of DNA suggest the AFM may soon provide an easier and faster technique for DNA sequencing.The AFM consists of a microfabricated SiO2 triangular shaped cantilever with a diamond tip affixed at the elbow to act as a probe. The sample is mounted on a electronically driven piezoelectric crystal. It is then placed in contact with the tip and scanned. The topography of the surface causes minute deflections in the 100 μm long cantilever which are detected using an optical lever.

The atomic-force microscope and its future in biology

1993 ◽  
Vol 51 ◽  
pp. 704-705
Author(s):  
Jean-Paul Revel
Keyword(s):  
Silicon Nitride ◽  
Laser Beam ◽  
Atomic Force Microscope ◽  
Scanning Tunneling Microscope ◽  
Point Of View ◽  
Scanning Tunneling ◽  
Close Relative ◽  
Tunneling Microscope ◽  
Atomic Force ◽  
Sharp Point

The last few years have been marked by a series of remarkable developments in microscopy. Perhaps the most amazing of these is the growth of microscopies which use devices where the place of the lens has been taken by probes, which record information about the sample and display it in a spatial from the point of view of the context. From the point of view of the biologist one of the most promising of these microscopies without lenses is the scanned force microscope, aka atomic force microscope.This instrument was invented by Binnig, Quate and Gerber and is a close relative of the scanning tunneling microscope. Today's AFMs consist of a cantilever which bears a sharp point at its end. Often this is a silicon nitride pyramid, but there are many variations, the object of which is to make the tip sharper. A laser beam is directed at the back of the cantilever and is reflected into a split, or quadrant photodiode.

The application of atomic force microscope in microbiological research

2014 ◽  
Vol 5 (1) ◽  
pp. 27-30
Author(s):  
Małgorzata Tokarska-Rodak ◽  
Maria Kozioł-Montewka ◽  
Jolanta Paluch-Oleś ◽  
Dorota Plewik ◽  
Grażyna Olchowik ◽  
...  
Keyword(s):  
Atomic Force Microscope ◽  
Atomic Force ◽  
Microbiological Research
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