scholarly journals Probing Surface Information of Alloy by Time of Flight-Secondary Ion Mass Spectrometer

Crystals ◽  
2021 ◽  
Vol 11 (12) ◽  
pp. 1465
Author(s):  
Tinglu Song ◽  
Meishuai Zou ◽  
Defeng Lu ◽  
Hanyuan Chen ◽  
Benpeng Wang ◽  
...  

In recent years, time of flight-secondary ion mass spectrometer (ToF-SIMS) has been widely employed to acquire surface information of materials. Here, we investigated the alloy surface by combining the mass spectra and 2D mapping images of ToF-SIMS. We found by surprise that these two results seem to be inconsistent with each other. Therefore, other surface characteristic tools such as SEM-EDS were further used to provide additional supports. The results indicated that such differences may originate from the variance of secondary ion yields, which might be affected by crystal orientation.

Author(s):  
B Kroell ◽  
S Starlinger ◽  
B Eitzinger

AbstractThe objective of this contribution is to characterise the distribution of adhesive between the plug wrap paper and the tipping paper on a finished cigarette. On the one hand, it is well known that this distribution influences various properties of the cigarette, but on the other hand, there are no methods available to completely determine this distribution. The area covered by adhesive, the amount of adhesive, and the thickness and position of the adhesive layer between the plug wrap and the tipping paper were chosen as essential quantities. Image analysis was used to evaluate the area covered by adhesive, and the amount of adhesive between the papers. The thickness and position of the adhesive layer were determined by processing pictures of paper cross-sections obtained with a time-of-flight secondary ion mass spectrometer (TOF-SIMS).


Author(s):  
Bruno Schueler ◽  
Robert W. Odom

Time-of-flight secondary ion mass spectrometry (TOF-SIMS) provides unique capabilities for elemental and molecular compositional analysis of a wide variety of surfaces. This relatively new technique is finding increasing applications in analyses concerned with determining the chemical composition of various polymer surfaces, identifying the composition of organic and inorganic residues on surfaces and the localization of molecular or structurally significant secondary ions signals from biological tissues. TOF-SIMS analyses are typically performed under low primary ion dose (static SIMS) conditions and hence the secondary ions formed often contain significant structural information.This paper will present an overview of current TOF-SIMS instrumentation with particular emphasis on the stigmatic imaging ion microscope developed in the authors’ laboratory. This discussion will be followed by a presentation of several useful applications of the technique for the characterization of polymer surfaces and biological tissues specimens. Particular attention in these applications will focus on how the analytical problem impacts the performance requirements of the mass spectrometer and vice-versa.


2020 ◽  
Author(s):  
Feifei Jia ◽  
Jie Wang ◽  
Yanyan Zhang ◽  
Qun Luo ◽  
Luyu Qi ◽  
...  

<p></p><p><i>In situ</i> visualization of proteins of interest at single cell level is attractive in cell biology, molecular biology and biomedicine, which usually involves photon, electron or X-ray based imaging methods. Herein, we report an optics-free strategy that images a specific protein in single cells by time of flight-secondary ion mass spectrometry (ToF-SIMS) following genetic incorporation of fluorine-containing unnatural amino acids as a chemical tag into the protein via genetic code expansion technique. The method was developed and validated by imaging GFP in E. coli and human HeLa cancer cells, and then utilized to visualize the distribution of chemotaxis protein CheA in E. coli cells and the interaction between high mobility group box 1 protein and cisplatin damaged DNA in HeLa cells. The present work highlights the power of ToF-SIMS imaging combined with genetically encoded chemical tags for <i>in situ </i>visualization of proteins of interest as well as the interactions between proteins and drugs or drug damaged DNA in single cells.</p><p></p>


1996 ◽  
Vol 122 (1-2) ◽  
pp. 1-15 ◽  
Author(s):  
Keyang Xu ◽  
Andrew Proctor ◽  
David M. Hercules

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