Proteome analysis by mass spectrometry.
The coupling of high-performance mass spectrometry instrumentation with highly efficient chromatographic and electrophoretic separations has enabled rapid qualitative and quantitative analysis of thousands of proteins from minute samples of biological materials. Here, we review recent progress in the development and application of mass spectrometry-based techniques for the qualitative and quantitative analysis of global proteome samples derived from whole cells, tissues, or organisms. Techniques such as multidimensional peptide and protein separations coupled with mass spectrometry, accurate mass measurement of peptides from global proteome digests, and mass spectrometric characterization of intact proteins hold great promise for characterization of highly complex protein mixtures. Advances in chemical tagging and isotope labeling techniques have enabled quantitative analysis of proteomes, and highly specific isolation strategies have been developed aimed at selective analysis of posttranslationally modified proteins.
Duke Scholars
Altmetric Attention Stats
Dimensions Citation Stats
Published In
DOI
EISSN
ISSN
Publication Date
Volume
Start / End Page
Related Subject Headings
- Spectroscopy, Fourier Transform Infrared
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
- Proteomics
- Proteome
- Proteins
- Mass Spectrometry
- Isotope Labeling
- Electrophoresis, Gel, Two-Dimensional
- Chromatography, High Pressure Liquid
- Chromatography, Affinity
Citation
Published In
DOI
EISSN
ISSN
Publication Date
Volume
Start / End Page
Related Subject Headings
- Spectroscopy, Fourier Transform Infrared
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
- Proteomics
- Proteome
- Proteins
- Mass Spectrometry
- Isotope Labeling
- Electrophoresis, Gel, Two-Dimensional
- Chromatography, High Pressure Liquid
- Chromatography, Affinity