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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Baez, Nelmi O. Devarie Reisz, Julie A. Furdui, Cristina M. |
| Description | Country affiliation: United States Author Affiliation: Baez NO ( Department of Internal Medicine, Section on Molecular Medicine, Wake Forest School of Medicine, Winston-Salem, NC 27157, USA.); Reisz JA ( Department of Internal Medicine, Section on Molecular Medicine, Wake Forest School of Medicine, Winston-Salem, NC 27157, USA.); Furdui CM ( Department of Internal Medicine, Section on Molecular Medicine, Wake Forest School of Medicine, Winston-Salem, NC 27157, USA. Electronic address: cfurdui@wakehealth.edu.) |
| Abstract | Mass spectrometry (MS) has become a powerful and widely utilized tool in the investigation of protein thiol chemistry, biochemistry, and biology. Very early biochemical studies of metabolic enzymes have brought to light the broad spectrum of reactivity profiles that distinguish cysteine thiols with functions in catalysis and protein stability from other cysteine residues in proteins. The development of MS methods for the analysis of proteins using electrospray ionization (ESI) or matrix-assisted laser desorption/ionization (MALDI) coupled with the emergence of high-resolution mass analyzers has been instrumental in advancing studies of thiol modifications, both in single proteins and within the cellular context. This article reviews MS instrumentation and methods of analysis employed in investigations of thiols and their reactivity toward a range of small biomolecules. A selected number of studies are detailed to highlight the advantages brought about by the MS technologies along with the caveats associated with these analyses. |
| File Format | HTM / HTML |
| ISSN | 08915849 |
| e-ISSN | 18734596 |
| DOI | 10.1016/j.freeradbiomed.2014.09.016 |
| Journal | Free Radical Biology and Medicine |
| Volume Number | 80 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2015-03-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Discipline Free radicals biology Cysteine Chemistry Peptide Fragments Proteins Sulfhydryl Compounds Animals Biocatalysis Kinetics Molecular Probes Oxidation-reduction Peptide Mapping Protein Stability Spectrometry, Mass, Electrospray Ionization Spectrometry, Mass, Matrix-assisted Laser Desorption-ionization Research Support, N.i.h., Extramural |
| Content Type | Text |
| Resource Type | Article |
| Subject | Physiology (medical) Biochemistry |
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