Mass spectrometry of protein and peptides

Mass spectrometry of protein and peptides /

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Bibliographic Details
Other Authors: Chapman, J. R.
Format: Book
Language:English
Published: Totowa, NJ : Humana Press, [2000]
Series:Methods in molecular biology (Clifton, N.J.) ; v. 146.
Methods in molecular biology ; 146.
Subjects:
Proteins > Analysis.
Peptides > Analysis.
Amino acid sequence.
Mass spectrometry.
Proteins.
Peptides.
Online Access:Publisher description
Available to Stanford-affiliated users at:
Table of Contents:
  • De Novo peptide sequencing by nanoelecrospray tandem mass spectrometry using triple quadrupole and quadrupole/time-of-flight instruments
  • Direct analysis of proteins in mixtures: application to protein complexes
  • Characterizaton of a mutant recombinant S100 protein using electrospray ionization mass spectrometry
  • Searching sequence databases via De Novo peptide sequencing by tandem mass spectrometry
  • Signature peptides: from analytical chemistry to functional genomics
  • Ivestigating the higher order structure of proteins: hydrogen exchange, proteolytic fragmentation, and mass spectrometry
  • Probing protein surface topology by chemical surface labeling, crosslinking, and mass spectrometry
  • Secondary structure of peptide ions in the gas phase evaluated by MIKE spectrometry: relevance to native conformations
  • Preparation and mass spectrometric analysis of S-nitrosohemoglobin
  • Multiple and subsequent MALDI-MS on-target chemical reactions for the characterization of dislfide bonds and primary structures of proteins
  • Epitope mapping by a combination of epitope excision and MALDI-MS
  • Identification of active site residues in glycosidases by use of tandem mass spectrometry
  • Probing protein-protein interactions with mass spectrometry
  • Studies of noncovalent complexes in an electrospray ionization/time-of-flight mass spectrometer
  • Kinetic analysis of enzymatic and nonenzymatic degradation of peptides by MALDI-TOFMS
  • Characterization of protein glycosylation by MALDI-TOFMS
  • Positive and negative labeling of human proinsulin, insulin and C-peptide with stable isotopes: new tools for in vivo pharmacokinetic and metabolic studies
  • Identification of snake species by toxin mass fingerprinting of their venoms
  • Mass spectrometric characterization of the [beta]-subunit of human chorionic gonadotropin
  • Analysis of gluten in foods by MALD-TOFMS
  • Quantitation of nucleotidyl cyclase and cyclic nucleotide-sensitive protein kinase activities by fast-atom bombardment mass spectrometry: a paradigm for multiple component monitoring in enzyme incubations by quantitative mass spectrometry
  • Influence of salts, buffers, detergents, solvents, and matrices on MALDI-MS protein analysis in complex mixtures
  • Sample preparation techniques for peptides and proteins analyzed by MALDI-MS
  • Analysis of hydrophobic proteins and peptides by mass spectrometry
  • Analysis of proteins and peptides directly from biological fluids by immunoprecipitation/mass spectrometry
  • Detection of molecular determinants in complex biological systems using MALDI-TOF affinity mass spectrometry
  • Rapid identification of bacteria based on spectral patterns using MALDI-TOFMS
  • Appendices.

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