## Abstract Some peptides have previously been reported to bind low molecular weight chemicals. One such peptide with the amino acid sequence HisโAlaโSerโTyrโSer was selectively screened from a phage library and bound to a cationic porphyrin, 5,10,15,20โtetrakis(__N__โmethylpyridiniumโ4โyl)โ21__H__
Tribological analysis of glass fibers using atomic force microscopy (AFM)/lateral force microscopy (LFM)
โ Scribed by N. Behary; A. Ghenaim; A. El Achari; C. Caze
- Publisher
- John Wiley and Sons
- Year
- 2000
- Tongue
- English
- Weight
- 434 KB
- Volume
- 75
- Category
- Article
- ISSN
- 0021-8995
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โฆ Synopsis
By using atomic force microscopy (AFM)/lateral force microscopy (LFM), a comparative study of the topography as well as the tribological properties (at a micrometer scale) of sized E-glass fibers was done. Normal and lateral deflection signals are recorded when an AFM tip scans a fiber surface. Friction force data were obtained from the forward and backward scans of lateral force images whose contrasts reveal differences in friction coefficient values and, hence, surface chemical heterogeneity of certainsized glass fibers. Sizes having an epoxy film former lead to a higher friction coefficient value than those containing a starch film former. Moreover, the epoxy-containing size is more readily plowed by the AFM tip. Annealing of this size lowers its friction coefficient.
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