Electrospray ionization is the main gentle ionization technique that interfaces with liquid chromatography

Gentle ionization techniques have revolutionized the field of mass spectrometry identification of proteins by providing an intact molecular ion that is facile to downstream analysis. One important gentle ionization technique is electrospray ionization (ESI) that remains the dominant technique that interface liquid chromatography with mass spectrometry. Specifically, in ESI, the protein analyte is pass through … More Electrospray ionization is the main gentle ionization technique that interfaces with liquid chromatography

Gentle ionization for mass spectrometry preserves the molecular ion and aids in compound identification

About 20 years ago, a suite of gentle ionization techniques such as electrospray ionization (ESI) and matrix assisted laser desorption/ionization (MALDI) are incorporated into commercial mass spectrometers, and revolutionized the way we detect and characterise the molecular ion. By molecular ion, we refer to the intact compound ion without any fragmentation. It can be seen … More Gentle ionization for mass spectrometry preserves the molecular ion and aids in compound identification

MALDI matrix helps transfer laser energy to ionize the biomolecules for mass spectrometric detection

Matrix assisted laser desorption ionization (MALDI) time of flight mass spectrometry is an established analytical technique for proteins, lipids, and biomolecules detection. But, there remains an “art” in this science technique. Specifically, scientists still do not have a thorough understanding of the ionization process in MALDI-TOF mass spectrometry. Such a situation leads to non-optimized protocols, … More MALDI matrix helps transfer laser energy to ionize the biomolecules for mass spectrometric detection

Mass spectrometry profiling of cellular proteome encounters the “missing proteome” problem

Proteome research received its first major enabling tool through the promulgation of two-dimensional gel electrophoresis. While the approach allows the separation of proteins based on molecular weight and isoelectric point, its chief bugbear remains in its semi-quantitative nature. This challenge was subsequently ameliorated by the introduction of mass spectrometry into proteomics, particularly with the advent … More Mass spectrometry profiling of cellular proteome encounters the “missing proteome” problem

Difficulty in quantifying the secretome of a cell

Bacterial cells secrete a variety of proteins and metabolites into the culture medium. This constitutes the secretome of a cell. Given that these proteins and metabolites are organic molecules, they should be amenable to separation and detection by liquid chromatography methods. However, given the complexity of the secretome and the matrix in which they are … More Difficulty in quantifying the secretome of a cell

Role of organic particles in seeding growth of aerosols in the atmosphere

Article in Nature, Vol. 533, 26 May 2016, pp. 527, “The role of low-volatility organic compounds in initial particle growth in the atmosphere”   Summary of article: Using nitrate ion chemical ionization atmospheric pressure interface time of flight mass spectrometry, a particle growth model for organic aerosols was proposed and validated.   Comment: Organic materials … More Role of organic particles in seeding growth of aerosols in the atmosphere

Mass spectrometry enables the identification of compounds that co-elute in column-based separation processes

Modern column-based separation processes such as high-performance liquid chromatography (HPLC) or gas chromatography (GC) possess high separation power that could provide clean separation of many types of compounds with the use of suitable column chemistry. However, there remains cases where two closely-related compounds such as a ketone and its corresponding alcohol co-elute as a single … More Mass spectrometry enables the identification of compounds that co-elute in column-based separation processes

Existence of ribosomal protein mass fingerprint of different bacterial, archaeal and eukaryotic species

Ribosomes are known to be highly conserved due to the importance of protein synthesis to cellular maintenance. Thus, constituent ribosomal proteins should theoretically be highly conserved, which implied a conserved amino acid sequence and molecular mass. However, unique molecular mass fingerprint of ribosomal proteins of individual species in the three domains of life was detected. … More Existence of ribosomal protein mass fingerprint of different bacterial, archaeal and eukaryotic species

General structure of the ribosome may be conserved, but small alterations in structural features likely exist between ribosomes of different species

Ribosome are highly conserved in structure and function given their importance to protein synthesis. Comprising a small and large subunit, ribosomes are built up of ribosomal proteins and RNA that provide both structure and function to the macromolecular complex.   Ribosomal proteins, in particular, differ in mass between different species and thus constitute a unique … More General structure of the ribosome may be conserved, but small alterations in structural features likely exist between ribosomes of different species

Conserved mass peaks in mass spectra of bacterial species

Conserved mass peaks were found in mass spectra of individual bacterial species that highlighted a deep biological basis in the use of mass spectrometry for identifying bacteria. Specifically, matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) could profile biomolecules (mostly proteins) from bacterial cells that result in a mass spectrum useful for identification purposes. While … More Conserved mass peaks in mass spectra of bacterial species