ChemInform Abstract: SECONDARY ION MASS SPECTROMETRY OF METAL HALIDES. 2. EVIDENCE FOR STRUCTURE IN ALKALI IODIDE CLUSTERS

1982 ◽  
Vol 13 (25) ◽  
Author(s):  
T. M. BARLAK ◽  
J. R. WYATT ◽  
R. J. COLTON ◽  
J. J. DECORPO ◽  
J. E. CAMPANA
Keyword(s):  
Mass Spectrometry ◽  
Secondary Ion Mass Spectrometry ◽  
Metal Halides ◽  
Ion Mass Spectrometry ◽  
Secondary Ion

Secondary ion mass spectrometry of metal halides. 3. Ionic radii effects in alkali halide clusters

1983 ◽  
Vol 87 (18) ◽  
pp. 3441-3445 ◽  
Author(s):  
Thomas M. Barlak ◽  
Joseph E. Campana ◽  
Jeffrey R. Wyatt ◽  
Richard J. Colton
Keyword(s):  
Mass Spectrometry ◽  
Alkali Halide ◽  
Secondary Ion Mass Spectrometry ◽  
Metal Halides ◽  
Ionic Radii ◽  
Ion Mass Spectrometry ◽  
Secondary Ion

Secondary ion mass spectrometry of metal halides. 1. Stability of alkali iodide clusters

1981 ◽  
Vol 85 (25) ◽  
pp. 3840-3844 ◽  
Author(s):  
T. M. Barlak ◽  
J. E. Campana ◽  
R. J. Colton ◽  
J. J. DeCorpo ◽  
J. R. Wyatt
Keyword(s):  
Mass Spectrometry ◽  
Secondary Ion Mass Spectrometry ◽  
Metal Halides ◽  
Ion Mass Spectrometry ◽  
Secondary Ion

Secondary ion mass spectrometry of metal halides. 2. Evidence for structure in alkali iodide clusters

1982 ◽  
Vol 104 (5) ◽  
pp. 1212-1215 ◽  
Author(s):  
T. M. Barlak ◽  
J. R. Wyatt ◽  
R. J. Colton ◽  
J. J. DeCorpo ◽  
J. E. Campana
Keyword(s):  
Mass Spectrometry ◽  
Secondary Ion Mass Spectrometry ◽  
Metal Halides ◽  
Ion Mass Spectrometry ◽  
Secondary Ion

Applications of Time-OF-Flight Secondary Ion Mass Spectrometry (TOF-SIMS)

1990 ◽  
Vol 48 (2) ◽  
pp. 308-309
Author(s):  
Bruno Schueler ◽  
Robert W. Odom
Keyword(s):  
Mass Spectrometry ◽  
Secondary Ion Mass Spectrometry ◽  
Structural Information ◽  
Time Of Flight ◽  
Biological Tissues ◽  
Polymer Surfaces ◽  
Tof Sims ◽  
Secondary Ions ◽  
Ion Mass Spectrometry ◽  
Secondary Ion

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.

Optics-Free Visualization of Proteins in Single Cells by Time of Flight-Secondary Ion Mass Spectrometry Coupled with Genetically Encoded Chemical Tags

2020 ◽  
Author(s):  
Feifei Jia ◽  
Jie Wang ◽  
Yanyan Zhang ◽  
Qun Luo ◽  
Luyu Qi ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Secondary Ion Mass Spectrometry ◽  
Single Cells ◽  
Time Of Flight ◽  
E Coli ◽  
Tof Sims ◽  
Ion Mass Spectrometry ◽  
Chemical Tags ◽  
Secondary Ion

<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>

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