Three Dimensional Analysis of a Grinding Wheel Surface with Image Processing

2012 ◽  
Vol 565 ◽  
pp. 177-182 ◽  
Author(s):  
Akihiro Sakaguchi ◽  
Tomoyuki Kawashita ◽  
Shuji Matsuo

It is very important to measure a grinding wheel surface topography. Therefore a three dimensional measurement system of grinding wheel surface with image processing has been proposed. This system can evaluate a variety of the wheel surface topographies. For example, a histogram of the area or the shape of cutting edges and the distribution map of every shape of cutting edges were obtained. In this paper, a three dimensional model of the cutting edges and a correlation between the state of the wheel surface and grinding mark on the workpiece are reported and the effectiveness is evaluated through an experiment.

2011 ◽  
Vol 325 ◽  
pp. 294-299 ◽  
Author(s):  
Akihiro Sakaguchi ◽  
Tomoyuki Kawashita ◽  
Shuji Matsuo

Grinding process is a very efficient machining technology because innumerable abrasive grains are fixed on the surface of grinding wheel. Especially, the distribution and shape of cutting edges which directly affect grinding process have a big influence on accuracy. Thus, it is very important to measure a wheel surface topography from a viewpoint of evaluating the wheel life and the performance and a relation between the one and the roughness. In this study, a three-dimensional measurement system of a grinding wheel surface with image processing is developed. In this system, the distribution and height of cutting edges are analyzed because only cutting edges can be selected from among all abrasive grains.


2003 ◽  
Vol 2003.40 (0) ◽  
pp. 197-198
Author(s):  
Osamu FURUYA ◽  
Satoshi Fujita ◽  
Yasushi Niitsu ◽  
Tadashi Mikoshiba ◽  
Daisuke Nakano ◽  
...  

Author(s):  
Walter E. Fowler ◽  
E. Loren Buhle ◽  
Ueli Aebi

Actin is known to specifically interact with a variety of intracellular proteins. Some of these interactions, for instance that of actin with myosin, are of obvious functional importance and have been extensively characterized, both biochemically and structurally. Other interactions, such as that of actin with DNase I, have not yet been correlated with specific cellular functions. In any case, the interaction between actin and DNase I has proven to be useful in both biochemical and structural studies. The two molecules form a tight 1:1 complex that inhibits the functions of both molecules: i.e. actin cannot polymerize into filaments any more and DNase I loses its enzymatic activity. The actin-DNase complex has been crystallized and a .6nm three-dimensional model of the complex has been obtained. Unfortunately, separation of the map into an actin and a DNase I part is ambiguous at this stage.


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