Advantages of Mass Spectrometry

Mass spectrometry has attained a unique position in analytical chemistry as a quantitative analysis tool, especially when coupled with high-resolution separation devices. Quantitative analysis of a variety of molecules is performed routinely with mass spectrometry-based methods at unprecedented high-sensitivity. It has several desirable features that make it the most sought-after analytical technique for quantitative analysis. These features include  

The field of quantitative analysis has been reviewed [1,2]. Quantitative analysis must be performed in compliance with good laboratory practices (GLPs) as defined by various regulatory agencies. This aspect has been discussed in a report in the Journal of American Society for Mass Spectrometry [3]. 

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Another advantage of mass spectrometry is its sensitivity - a full-scan spectrum, and potentially an identification, can be obtained from picogram (pg) amounts of analyte. In addition, it may be used to provide quantitative information, usually to low levels, with high accuracy and precision. 

While mass spectrometry cannot provide the detailed structural information that is obtained by NMR and X-ray crystallography, it can, in principle, provide valuable information on the formation and stoichiometry of nonco-valent complexes. There are several key questions that need to be addressed before we can decide whether the advantages of mass spectrometry (sensitivity, speed, and specificity) can be successfully applied to the study of nonco-valent interactions. These questions are... 

An important advantage of mass spectrometry over other techniques such as electrophoresis or chromatography is its high speed. For instance, the association of MALDI/TOF with automatic preparation of the samples, together with automated acquisition of the spectra, allows the analysis of more than 100 oligonucleotides in 90 min. [172]... 

Another important advantage of mass spectrometry is its capacity to verify the incorporation of modified nucleotides. Figure 8.31 displays the mass spectrum of a synthetic oligonucleotide whose theoretical mass is 5838 Da. In addition to the desired nucleotide, other compounds are present. The mass difference between the peaks (111-151 Da) corresponds to the masses of the nucleic bases. This suggests that depurination reactions have occurred during the synthesis. 

Specific advantages of mass spectrometry in peptide sequencing... 

Mass spectrometry has become a major player in proteome analysis because of its integration with high-resolution separation techniques and protein databases and its inherent high sensitivity, high structure specificity, high-mass capability, and opportunity for automation. Short analysis times and straightforward sample preparation steps are the other advantages of mass spectrometry-based proteomics. 

The Advantages of Mass Spectrometry for Genetic Diversity Detection. ... 

One of the great advantages of mass spectrometry is that it can work with extremely small samples, less than 10 of a mole. It is often used coupled to a gas-liquid chromatography analyser, and the separated fractions are run automatically into the mass spectrometer. It is particularly valuable for the study of biological samples. 

In most cases, standards are also needed for analysis, and these should be added to the sample as soon as possible, preferably at the time of sampling. The standard is often an isotope-labeled compound. A big advantage of mass spectrometry-based methods is that they can detect stable isotope labels and are not radioactive therefore, they do not pose a health hazard and can be freely used. Stable isotope labeling is also called isotope labeled affinity tags, especially in the field of proteomics. 

There are many binary systems whose vapour contains mixed associates and a large number of vapour species. The virtue of the KSMC method is the possibility of directly determining the partial pressures of vapour species, rather than the total pressure in the system. These advantages of mass spectrometry are widely used in thermodynamic research into two-component systems. If there are mixed species A B and Afis in the saturated vapour of system A-B, the Gibbs-Duhem equation jNjd In aj = 0 can be written as... 

In the first part of this chapter we will briefly discuss the nature of noncovalent interactions, followed by an overview of standard methods for probing them (optical and fluorescence spectroscopy, isothermal titration calorimetry/microcalorimetry, differential scanning calorimetry, and surface plasmon resonance), with particular attention to their application to biomolecules. An overview of mass spectrometric methods suitable for detecting noncovalent complexes will then be presented. The advantages of mass spectrometry compared with conventional analytical methods are sensitivity, speed, and the ability to obtain stoichiometric information directly. 

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