Protein Sequencing and Identification Using Tandem Mass by Michael Kinter

By Michael Kinter

How to layout, execute, and interpret experiments for protein sequencing utilizing mass spectrometry

The fast enlargement of searchable protein and DNA databases lately has caused an explosive development within the program of mass spectrometry to protein sequencing. This well timed and authoritative booklet presents execs and scientists in biotechnology learn with whole assurance of techniques for studying protein sequences through mass spectrometry, together with step by step instructions for pattern education, research, and knowledge interpretation.

Michael Kinter and Nicholas Sherman current their very own top quality, laboratory-tested protocols for the research of a large choice of samples, demonstrating how one can perform particular experiments and acquire speedy, trustworthy effects with a ninety nine% luck expense. Readers gets enough experimental element to use of their personal laboratories, know about the right kind choice and operation of tools, and achieve crucial perception into the basic ideas of mass spectrometry and protein sequencing. insurance includes:

  • Peptide fragmentation and interpretation of product ion spectra
  • Basic polyacrylamide gel electrophoresis
  • Preparation of protein digests for sequencing experiments
  • Mass spectrometric research utilizing capillary liquid chromatography
  • Techniques for protein id by way of database searches
  • Characterization of transformed peptides utilizing tandem mass spectrometry

And a lot more

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Science 246:667 1, 1989. 5. 63. T. Electrospray ionization mass spectrometric peptide mapping: A rapid, sensitive technique for protein structure analysis. Biochem. Biophys. Res. Comm. 167:686-692, 1990. 64. ; Watanabe C. Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases. Proc. Natl. Acad. Sci. A. 90:5011-5015, 1993. 65. ; Hunkapiller, T. Peptide mass maps: A highly informative approach to protein identification. Anal. Biochem.

Partial primary structure of bacteriorhodopsin: Sequencing methods for membrane proteins. Proc. Natl. Acad. Sci. U S A . 76:227-231, 1979. 35. ; Biemann, K. Amino acid sequence of bacteriorhodopsin. Proc. Natl. Acad. Sci. U S A . 7615046-5050, 1979. 36. G. The site of attachment of retinal in bacteriorhodopsin. The epsilon-amino group in Lys-41 is not required for proton translocation. 1 Biol. Chem. 257:8596-8599, 1982. 37. ; Titani, K. n-Tetradecanoyl is the NH2-terminal blocking group of the catalytic subunit of cyclic AMP-dependent protein kinase from bovine cardiac muscle.

10. J. A gas-liquid solid phase peptide and protein sequenator. 1 Biol. Chem. 256:7990-7997, 1981. 11. ; van Montagu, M. Proteinblotting on Polybrene-coated glass-fiber sheets. A basis for acid hydrolysis and gasphase sequencing of picomole quantities of protein previously separated on sodium dodecyl sulfate/polyacrylamide gel. Eur: 1 Biochem. 152:9-19, 1985. 12. H. Electroblotting onto activated glass. High efficiency preparation of proteins from analytical sodium dodecyl sulfatepolyacrylamide gels for direct sequence analysis.

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