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• W1499120045 abstract "Innovations in mass spectrometry (MS) have greatly advanced the ability to sequence and study the structures of proteins. In particular, protein analysis strategies have greatly benefited from the introduction of electrospray ionization. This chapter discusses peptide and protein analysis by mass spectrometry and instrumentation and strategies, employing tandem mass spectrometers are described. Significant instrumental improvements in both cost and performance are to be expected as several types of mass spectrometers reach a level of refinement that permits commercial versions to be introduced. Ion trap mass spectrometers are increasingly used for the analysis of biomolecules, with greater sensitivity and mass resolution, than quadrupole mass spectrometers. Sequence information for peptides can now be obtained on reflectron time-of-flight mass spectrometers and improvements in the ability to scan the reflectron voltages are expected. Improvements in surface-induced dissociation (SID) have been achieved, by coating metal surfaces, with self-assembled monolayers, greatly increasing the efficiency of fragment ion recovery from the surface. In addition, fragment ions have been observed in SID studies of peptides that allow the differentiation of leucine and isoleucine on quadrupole-type mass spectrometers. These developments ensure that mass spectrometry continues to have a significant role in biological research." @default.
• W1499120045 created "2016-06-24" @default.
• W1499120045 creator A5083768832 @default.
• W1499120045 date "1996-01-01" @default.
• W1499120045 modified "2023-10-18" @default.
• W1499120045 title "[15] Protein structure analysis by mass spectrometry" @default.
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• W1499120045 doi "https://doi.org/10.1016/s0076-6879(96)71017-0" @default.
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