Matrix-assisted laser desorption/ionization mass spectrometry of biopolymers

Hillenkamp, Franz; Karas, Michael; Beavis, Ronald C.; Chait, Brian T.

doi:10.1021/ac00024a002

Cited by 1,096 publications

(805 citation statements)

References 36 publications

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“…[2] Molecular information on organic, inorganic and biological molecules can be deduced from the accurately measured masses of the molecules of interest and their fragments. [1,6] The ground-breaking developments of soft ionization methods in biological MS in the 1980s, namely electrospray ionization (ESI) [7] and matrix-assisted laser desorption ionization (MALDI), [8] have tremendously accelerated the development of analytical instrumentation and data analysis tools for species of biological importance, leading to the recognition of ESI and MALDI developments with a Nobel Prize in Chemistry in 2002. Particularly, significant investments have been made in the area of the MS-based life sciences applications, especially systems biology-oriented ones.…”

mentioning

confidence: 99%

High-Resolution and Tandem Mass Spectrometry – the Indispensable Tools of the XXI Century

Tsybin

Fornelli²,

Kozhinov³

et al. 2011

Chimia

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Mass spectrometry-based qualitative and quantitative (bio)molecular analysis is a corner stone in the state-of-the-art pipelines in systems biology and environmental sciences. High-resolution and efficient tandem mass spectrometry methods and techniques are the essential analytical capabilities for the in-depth analysis of extremely complex mixtures of (bio)molecules of a very broad dynamic range of concentrations. Here, we briefly review the advantages and limitations of the current mass spectrometry with a focus on resolution, or resolving power, and methods of (bio)molecular fragmentation in the gas phase. We conclude with an outlook that considers possible avenues for further mass spectrometry-based method and technique development, indispensable for advancing the challenging real-life mass spectrometry applications in the XXI century.

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mentioning

confidence: 99%

High-Resolution and Tandem Mass Spectrometry – the Indispensable Tools of the XXI Century

Tsybin

Fornelli²,

Kozhinov³

et al. 2011

Chimia

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show abstract

“…One of the most important developments in instrumentation has been the introduction of “soft-ionization” technology, which permits proteins and peptides to be analyzed by MS. Proteins and peptides are polar, nonvolatile species that require an ionization method to transfer them into the gas phase, without extensive degradation. Two techniques paved the way for the modern bench-top MS proteomics: matrix-assisted laser desorption ionization (MALDI) [46,47] and electrospray ionization (ESI) [48]. In a MALDI source, peptides are co-crystallized with a solid-phase matrix onto a metal plate.…”

Section: Fundamentals Of Mass Spectrometry Technologymentioning

confidence: 99%

Mass Spectrometry-Based Proteomics for the Analysis of Chromatin Structure and Dynamics

Soldi

Cuomo

Bremang

et al. 2013

IJMS

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Chromatin is a highly structured nucleoprotein complex made of histone proteins and DNA that controls nearly all DNA-dependent processes. Chromatin plasticity is regulated by different associated proteins, post-translational modifications on histones (hPTMs) and DNA methylation, which act in a concerted manner to enforce a specific “chromatin landscape”, with a regulatory effect on gene expression. Mass Spectrometry (MS) has emerged as a powerful analytical strategy to detect histone PTMs, revealing interplays between neighbouring PTMs and enabling screens for their readers in a comprehensive and quantitative fashion. Here we provide an overview of the recent achievements of state-of-the-art mass spectrometry-based proteomics for the detailed qualitative and quantitative characterization of histone post-translational modifications, histone variants, and global interactomes at specific chromatin regions. This synopsis emphasizes how the advances in high resolution MS, from “Bottom Up” to “Top Down” analysis, together with the uptake of quantitative proteomics methods by chromatin biologists, have made MS a well-established method in the epigenetics field, enabling the acquisition of original information, highly complementary to that offered by more conventional, antibody-based, assays.

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“…Matrix-assisted laser desorption-ionization (MALDI), the second 'soft ionization' technique uses irradiation by a laser to desorb intact molecular ions usually proteins/peptides or DNA that are co-crystallized in a photoactive matrix solution. 11,12 Unlike the ESI process, which generates multiply charged ions, in MALDI typically only singly charged ions are observed. In this technique the analyte is co-crystallized with an excess of matrix, which absorbs UV light from a laser thus facilitating analyte desorption and ionization.…”

Section: Mass Analyzersmentioning

confidence: 99%

“…Analyte molecules are vaporized along with the matrix producing gas phase ions that are then accelerated in an electric field until they reach the detector Figure 2B. 11,12 The high throughput potential and relative ease of use of MALDImass spectrometers have made them attractive machines for the screening of clinical samples for biomarkers.…”

Section: Mass Analyzersmentioning

confidence: 99%

Proteomics in the microbial sciences

Graham¹,

McMullan²,

Graham³

2011

Bioengineered Bugs

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Mass spectrometry based proteomics is now widely used in the microbial sciences. In conjunction with transcriptomics it has greatly enhanced the field of microbial biology and has provide microbiologists with unparalleled insights into cellular processes and functions. Proteomics allows the dynamic nature of the entire protein network to be mapped providing a deeper understanding of microbial systems, their evolution and role in disease states. This review is intended to provide an overview of mass spectrometry and its application to the field of microbial proteomics. Background is provided on the core mass analyzers, including the Orbitrap mass spectrometer, and novel fragmentation processes such as Electron Transfer Dissociation which leave post-translational modifications intact on peptide backbones allowing for their identification and localization. The review will also provide information on current key quantitative technologies and the state of the art in microbial metaproteomics.

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Matrix-assisted laser desorption/ionization mass spectrometry of biopolymers

Cited by 1,096 publications

References 36 publications

High-Resolution and Tandem Mass Spectrometry – the Indispensable Tools of the XXI Century

High-Resolution and Tandem Mass Spectrometry – the Indispensable Tools of the XXI Century

Mass Spectrometry-Based Proteomics for the Analysis of Chromatin Structure and Dynamics

Proteomics in the microbial sciences

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