Microdispersion of Carbon Blacks in Rubber, Part I: Some Quantitative Aspects by AFM Image Analysis

2006 ◽  
Vol 79 (5) ◽  
pp. 783-789 ◽  
Author(s):  
C. C. Wang ◽  
S. H. Wu ◽  
J. B. Donnet ◽  
T. K. Wang
Keyword(s):  
Particle Size ◽  
Atomic Force Microscopy ◽  
Image Analysis ◽  
Force Microscopy ◽  
Carbon Blacks ◽  
Surface Fraction ◽  
Atomic Force ◽  
Distance Distributions ◽  
Rubber Part ◽  
Afm Image

Abstract The microdispersion state of carbon blacks in an emulsion SBR matrix has been observed by atomic force microscopy (AFM) and the images analyzed quantitatively. The fillers were well dispersed in the rubber samples. Different parameters, such as the surface fraction of fillers in images, particle size distance distributions, have been extracted and the main results are presented.

Interrogation of Alumina Grain Boundaries using Atomic Force Microscopy

1999 ◽  
Vol 580 ◽  
Author(s):  
P.A. Tibble ◽  
B.R. Heywood ◽  
R. Richardson ◽  
P. Barnes
Keyword(s):  
Particle Size ◽  
Atomic Force Microscopy ◽  
Grain Boundary ◽  
Grain Boundaries ◽  
Preferential Growth ◽  
Polycrystalline Alumina ◽  
Present Evidence ◽  
Force Microscopy ◽  
Atomic Force ◽  
Uniform Growth

AbstractA number of MgO doped (3wt%) polycrystalline alumina samples were prepared. The preparation of these samples varied; different regimes for annealing (1500 – 1600°C) and a range of dwell times were examined. Atomic force microscopy (AFM) was used to study surface features. Information on grain boundary dimensions (depth, width) is presented along with a study of grain particle size. The growth of the grain boundaries was found to contradict Mullins' theory of uniform growth with time. We also present evidence for Ostwalds' ripening and the preferential growth of [001] oriented grains.

scholarly journals Gloss phenomena and image analysis of atomic force microscopy in molecular and cell biology

Scanning ◽  
2009 ◽  
Vol 31 (2) ◽  
pp. 49-58 ◽  
Author(s):  
Jie Zhu ◽  
Tanya Sabharwal ◽  
Lianhong Guo ◽  
Aruna Kalyanasundaram ◽  
Guodong Wang
Keyword(s):  
Atomic Force Microscopy ◽  
Image Analysis ◽  
Cell Biology ◽  
Force Microscopy ◽  
Atomic Force

scholarly journals Assessment of the Scales of Gilthead Seabream (Sparus aurata L.) by Image Analysis and Atomic Force Microscopy

Fishes ◽  
2018 ◽  
Vol 3 (1) ◽  
pp. 9
Author(s):  
Francisco Casado ◽  
Santiago Casado ◽  
Diana Ceballos-Francisco ◽  
María Esteban
Keyword(s):  
Atomic Force Microscopy ◽  
Image Analysis ◽  
Sparus Aurata ◽  
Gilthead Seabream ◽  
Force Microscopy ◽  
Atomic Force

scholarly journals Structural identification of individual helical amyloid filaments by integration of cryo-electron microscopy-derived maps in comparative morphometric atomic force microscopy image analysis

2021 ◽  
Author(s):  
Liisa Lutter ◽  
Youssra Al-Hilaly ◽  
Christopher J. Serpell ◽  
Mick F. Tuite ◽  
Claude M. Wischik ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Atomic Force Microscopy ◽  
Image Analysis ◽  
Structural Analysis ◽  
Amyloid Fibrils ◽  
Structural Identification ◽  
Force Microscopy ◽  
Atomic Force ◽  
Cryo Electron Microscopy

The presence of amyloid fibrils is a hallmark of more than 50 human disorders, including neurodegenerative diseases and systemic amyloidoses. A key unresolved challenge in understanding the involvement of amyloid in disease is to explain the relationship between individual structural polymorphs of amyloid fibrils, in potentially mixed populations, and the specific pathologies with which they are associated. Although cryo-electron microscopy (cryo-EM) and solid-state nuclear magnetic resonance (ssNMR) spectroscopy methods have been successfully employed in recent years to determine the structures of amyloid fibrils with high resolution detail, they rely on ensemble averaging of fibril structures in the entire sample or significant subpopulations. Here, we report a method for structural identification of individual fibril structures imaged by atomic force microscopy (AFM) by integration of high-resolution maps of amyloid fibrils determined by cryo-EM in comparative AFM image analysis. This approach was demonstrated using the hitherto structurally unresolved amyloid fibrils formed in vitro from a fragment of tau (297-391), termed 'dGAE'. Our approach established unequivocally that dGAE amyloid fibrils bear no structural relationship to heparin-induced tau fibrils formed in vitro. Furthermore, our comparative analysis resulted in the prediction that dGAE fibrils are closely related structurally to the paired helical filaments (PHFs) isolated from Alzheimer's disease (AD) brain tissue characterised by cryo-EM. These results show the utility of individual particle structural analysis using AFM, provide a workflow of how cryo-EM data can be incorporated into AFM image analysis and facilitate an integrated structural analysis of amyloid polymorphism.

Subsurface Image Analysis of Plant Cell Wall with Atomic Force Microscopy

2013 ◽  
Vol 8 (2) ◽  
pp. 100-104
Author(s):  
Sahar Maghsoudy-Louyeh ◽  
Jeong Kim ◽  
Matthew Kropf ◽  
Bernhard Tittmann
Keyword(s):  
Atomic Force Microscopy ◽  
Cell Wall ◽  
Image Analysis ◽  
Plant Cell ◽  
Plant Cell Wall ◽  
Force Microscopy ◽  
Atomic Force
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