Chromatography Techniques and Spectrometry

Mass Spectrometry for Proteomics

Study of all proteins in a biological system during specific biological events is known as Proteomics (e.g., cells, tissue, and organism). Because of the dynamic nature of protein expression, to study Genomics and proteomics together are considerably more difficult than genomics or even transcriptomics alone. Additionally, some form of posttranslational modification (PTM) will be undergone by the majority of proteins, further increasing proteomic complexity. Due in large part to technological developments in mass spectrometry the broad scope of proteomics is only beginning to be realized during the last 15 years.

To detect, identify and quantitate molecules based on their mass-to-charge (m/z) ratio, Mass spectrometry is a sensitive technique used. to trace heavy isotopes through biological systems, MS was first used in the biological sciences, originally to measure elemental atomic weights and the natural abundance of specific isotopes developed almost 100 years ago. In later years, to sequence oligonucleotides and peptides and analyze nucleotide structure MS was used. The study of protein structure by MS was enabled by the development of macromolecule ionization methods, including electrospray ionization (ESI) and atmospheric pressure chemical ionization (APCI).  To obtain protein mass "fingerprints" that could be matched to proteins and peptides in databases and helped and allowed scientists to trace out identity of unknown targets, by Ionization. Both in relative and absolute quantities new isotopic tagging methods led to the quantitation of target proteins. All these technological advancements have resulted in methods that successfully analyze samples in solid, liquid or gas states. The attomolar range (10-18) is the sensitivity of current mass spectrometers allows one to detect analytes of different concentrations.