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113 Applications of Mass Spectrometry in Bio-analytical ChemistryAmong all mass spectrometry applications the bio-analytical applications have been paid the most attention to in the past decade A biological sample usually contains several categories of molecules including DNARNA protein lipids and other small molecules After the development of genome research people start to investigate into the other components inside a cell Although MS have been used to analyze biologically interested compounds such as peptide in as early as 1966 it did not become a main application until combined with soft ionization methods such as ESI and MALDI Soft ionization methods preserve most of the precursor ion information makes it possible to ionize large bio-molecules without breaking the chemical bonds Therefore they have become a standard method for analyzing complex biological samples Here only a few bio-analytical applications that are related to this dissertation are briefly reviewedOne kind of the complex biological samples is from proteomic research Protein acts as the functional factory inside a cell It functions as carriers enzymes gates and so on Genome might be the same in both healthy and unhealthy human body but the proteins functioning could be different Certain protein might be increased or decreased other might even not exist Studying the protein in a biological sample will help people in understanding how disease functions locating healthy and non-healthy organs and even finding protein biomarkers This might lead to curing the disease The large-scale study of proteins particularly their structure and functions is defined as proteomics In proteomics studies two types of mass spectrometry experiments are commonly used11 Protein or peptide could be ionized and the mass could be recorded by MS1 experiments The structural information could be obtained by analyzing the fragment ions from tandem mass scan MSMS or MS2 Mass spectrometry based proteomics could identify the sequence of a protein through the fragmentation detect the post translation modification and give information about tertiary structure of protein through methods such
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