## Abstract Matrixβassisted laser desorption/ionization mass spectrometry (MALDIβMS) has been successfully applied to elucidating biological questions trough the analysis of proteins, peptides, and nucleic acids. Here, we review the different approaches for analyzing the data that is generated by M
Informatics for mass spectrometry-based RNA analysis
β Scribed by Hiroshi Nakayama; Nobuhiro Takahashi; Toshiaki Isobe
- Publisher
- John Wiley and Sons
- Year
- 2011
- Tongue
- English
- Weight
- 802 KB
- Volume
- 30
- Category
- Article
- ISSN
- 0277-7037
No coin nor oath required. For personal study only.
β¦ Synopsis
Abstract
Mass spectrometry (MS) allows the sensitive and direct characterization of biological macromolecules and therefore has the potential to complement the more conventional genetic and biochemical methods used for RNA characterization. Although MS has been used much less frequently for RNA research than it has been for protein research, recent technical improvements in both instrumentation and software make MS a powerful tool for RNA analysis because it can now be used to sequence, quantify, and chemically analyze RNAs. Mass spectrometry is particularly well suited for the characterization of RNAs associated with ribonucleoprotein complexes. This review focuses on the software and databases that can be used for MSβbased RNA studies. Software for the processing of raw mass spectra, the identification and characterization of RNAs by mass mapping, de novo sequencing, and tandem MSβbased database searching are available. Β© 2010 Wiley Periodicals, Inc., Mass Spec Rev 30:1000β1012, 2011
π SIMILAR VOLUMES
Mass spectrometry in combination with tracer experiments based on 13 C substrates can serve as a powerful tool for the modeling and analysis of intracellular fluxes and the investigation of biochemical networks. The theoretical background for the application of mass spectrometry to metabolic flux an
## Abstract Microfluidic devices coupled to mass spectrometers have emerged as excellent tools for solving the complex analytical challenges associated with the field of proteomics. Current proteome identification procedures are accomplished through a series of steps that require many hours of labo
The most demanding problems in proteomics continue to challenge modern mass spectrometry. Recent developments in instrument design have led to lower limits of detection, while new ion activation techniques and improved understanding of gas-phase ion chemistry have enhanced the capabilities of tandem