Record Display for the EPA National Library Catalog

RECORD NUMBER: 32 OF 41

OLS Field Name OLS Field Data
Main Title Protein sequencing and identification using tandem mass spectrometry /
Author Kinter, Michael.
Other Authors
Author Title of a Work
Sherman, Nicholas E.
Publisher John Wiley,
Year Published 2000
OCLC Number 43798507
ISBN 0471322490 (cloth : alk. paper); 9780471322498 (cloth : alk. paper)
Subjects Nucleotide sequence. ; Proteins--Analysis. ; Mass spectrometry. ; Eiwitten. ; Nucleotiden. ; Massaspectrometrie. ; Fragmentatie. ; Elektroforese. ; Sequence Analysis, Protein. ; Mass Spectrometry. ; Proteins--analysis. ; Sâequence nuclâeotidique. ; Protâeines--Identification. ; Spectroscopie de masse. ; Spectrum Analysis, Mass
Internet Access
Description Access URL
http://www.loc.gov/catdir/bios/wiley043/00038204.html
http://www.loc.gov/catdir/description/wiley036/00038204.html
Contributor biographical information http://catdir.loc.gov/catdir/bios/wiley043/00038204.html
Publisher description http://catdir.loc.gov/catdir/description/wiley036/00038204.html
Holdings
Library Call Number Additional Info Location Last
Modified
Checkout
Status
EKBM  QP551.K495 2000 Research Triangle Park Library/RTP, NC 05/07/2004
EKCM  QP551.K495 2000 NHEERL/GED Library/Gulf Breeze,FL 02/01/2006
ELBM  QP551.K495 2000 AWBERC Library/Cincinnati,OH 08/01/2011
Collation xvi, 301 p. : ill. ; 24 cm.
Notes
Includes bibliographical references and index.
Contents Notes
An introduction to protein sequencing using tandem mass spectrometry -- The primary structure of proteins and a historical overview of protein sequencing -- Fundamental mass spectrometry -- Collisionally induced dissociation of protonated peptide icons and the interpretation of product ion spectra -- Basic polyacrylamide gel electrophoresis -- The preparation of protein digests for mass spectrometric sequencing experiments -- Mass spectrometric analysis of tryptic digests -- Protein identification by database searching -- Sequence analysis of novel proteins -- The characterization of post-translationally modified proteins using tandem mass spectometry.