Mass spectrometry of biomolecules

Advances in mass spectrometry have made it a tool of exceptional power for analysis of large biomolecules. Electrospray ionization, MALDI, and other soft ionization techniques for nonvolatile compounds and macromolecules make possible analyses of proteins, nucleic acids, and other biologically relevant compounds with molecular weights up to and in excess of 100,000 daltons. Electrospray ionization with quadrupole mass analysis is now routine for biomolecule analysis as is analysis using MALDI-TOF instruments. Extremely high resolution can be achieved using Fourier transform-ion cyclotron resonance (FT ICR, or FTMS). We shall discuss ESI and MALDI applications of mass spectrometry to protein sequencing and analysis in Sections 24.5E, 24.13B, and 24.14. 

The key terms and concepts that are highlighted in bold, blue text within the chapter are wil y  

Chapter 9 Nuclear Magnetic Resonance and Mass Spectrometry 

B l rc l ote to Instructors Many of the homework problems are available for assignment via WileyPLUS, an online r L U O teaching and learning solution. 

The following are some abbreviations used to report spectroscopic data  

---

R. D. Macfarlane. Mass Spectrometry of Biomolecules From PDMS to MALDI. Brazilian J. Phys., 29(1999) 415-420. 

B. Spengler. Post-Source Decay Analysis in Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry of Biomolecules. J. Mass Spectrom., 32(1997) 1019-1036. 

Spengler, B. (1 997) Post-source decay analysis in matrix-assisted laser desorption/ionization mass spectrometry of biomolecules. Journal of Mass Spectrometry 32, 1019-1036. 

V. A. Pokrovskiy. Temperature-programmed desorption mass spectrometry of biomolecules, Rapid Commun. Mass Spectrom. 9, 588-591 (1995). 

Mass Spectrometry of Biomolecules 444 [ WHY DO THESE TOPICS MATTER ] 444... 

---