scholarly journals Mass spectrometry of modified RNAs: recent developments

The Analyst ◽  
2016 ◽  
Vol 141 (1) ◽  
pp. 16-23 ◽  
Author(s):  
Collin Wetzel ◽  
Patrick A. Limbach
Keyword(s):  
Mass Spectrometry ◽  
Complex Mixtures ◽  
Chemical Modifications ◽  
Quantitative Characterization ◽  
Ribonucleic Acids ◽  
Recent Developments

A common feature of ribonucleic acids (RNAs) is that they can undergo a variety of chemical modifications, all of which can be detected by mass spectrometry. Here we highlight recent analytical developments in the field, which now enable quantitative characterization of complex mixtures of modified RNAs.

scholarly journals The emerging interface of mass spectrometry with materials

2019 ◽  
Vol 11 (1) ◽  
Author(s):  
Papri Chakraborty ◽  
Thalappil Pradeep
Keyword(s):  
Mass Spectrometry ◽  
Photoelectron Spectroscopy ◽  
Noble Metals ◽  
Vacuum Ultraviolet ◽  
Materials Science ◽  
Modern Science ◽  
Structural Details ◽  
Recent Developments ◽  
Characterization Of Materials

Abstract Mass spectrometry (MS), a hundred-year-old subject, has been a technique of profound importance to molecular science. Its impact in solid-state materials science has not been evident, although many materials of modern science, such as fullerenes, have their origins in MS. Of late, mass spectrometric interface with materials is increasingly strengthened with advances in atomically precise clusters of noble metals. Advances in instrumentation along with recent developments in synthetic approaches have expanded the chemistry of clusters, and new insights into matter at the nanoscale are emerging. High-resolution MS coupled with soft ionization techniques enable efficient characterization of atomically precise clusters. Apart from that, techniques such as ion mobility, tandem MS, etc. reveal structural details of these systems. Growth, nucleation, and reactivity of clusters are also probed by MS. Some of the recent advancements in this field include the development of new hyphenated techniques. Finer structural details may be obtained by coupling MS with spectroscopic tools, such as photoelectron spectroscopy, vacuum ultraviolet spectroscopy, etc. With such advancements in instrumentation, MS can evolve into a universal tool for the characterization of materials. The present review captures highlights of this area.

The characterization of complex mixtures by field desorption-tandem mass spectrometry

1998 ◽  
Vol 12 (23) ◽  
pp. 1914-1924 ◽  
Author(s):  
Anthony T. Jackson ◽  
Richard C. K. Jennings ◽  
James H. Scrivens ◽  
Martin R. Green ◽  
Robert H. Bateman
Keyword(s):  
Mass Spectrometry ◽  
Tandem Mass Spectrometry ◽  
Complex Mixtures ◽  
Tandem Mass ◽  
Field Desorption

Application of Mass Spectrometry in Proteomics

2005 ◽  
Vol 25 (1-2) ◽  
pp. 71-93 ◽  
Author(s):  
Ida Chiara Guerrera ◽  
Oliver Kleiner
Keyword(s):  
Mass Spectrometry ◽  
Mass Measurement ◽  
Mass Spectrometric ◽  
Protein Isoforms ◽  
Complex Mixtures ◽  
Spectrometric Analysis ◽  
Specific Information ◽  
Stable Isotope Labelling ◽  
Core Technology ◽  
Recent Developments

Mass spectrometry has arguably become the core technology in proteomics. The application of mass spectrometry based techniques for the qualitative and quantitative analysis of global proteome samples derived from complex mixtures has had a big impact in the understanding of cellular function. Here, we give a brief introduction to principles of mass spectrometry and instrumentation currently used in proteomics experiments. In addition, recent developments in the application of mass spectrometry in proteomics are summarised. Strategies allowing high-throughput identification of proteins from highly complex mixtures include accurate mass measurement of peptides derived from total proteome digests and multidimensional peptide separations coupled with mass spectrometry. Mass spectrometric analysis of intact proteins permits the characterisation of protein isoforms. Recent developments in stable isotope labelling techniques and chemical tagging allow the mass spectrometry based differential display and quantitation of proteins, and newly established affinity procedures enable the targeted characterisation of post-translationally modified proteins. Finally, advances in mass spectrometric imaging allow the gathering of specific information on the local molecular composition, relative abundance and spatial distribution of peptides and proteins in thin tissue sections.

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