Proteome Characterization and ProteomicsTimothy D. Veenstra, Richard D. Smith The content of this volume is designed to reach a wide audience, including those involved with relevant technologies such as electrophoresis and mass spectrometry, to those interested in how proteomics can benefit research. A wide range of techniques are discussed, each specifically designed to address different needs in proteomic analysis. The concluding chapter discusses the important issue related to handling large amounts of data accumulated in proteomic studies.
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Page 10
... ion trap MS technologies. The high MMA achievable with FTICR will allow the use of proteolytic fragments as biomarkers or accurate mass tags (AMTs) to uniquely identify a protein; an approach that is robust because of its amenability to ...
... ion trap MS technologies. The high MMA achievable with FTICR will allow the use of proteolytic fragments as biomarkers or accurate mass tags (AMTs) to uniquely identify a protein; an approach that is robust because of its amenability to ...
Page 20
... ion cyclotron resonance mass spectrometry. Anal. Chem. 71, 2076–2084. Jonscher, K. R., and Yates, J. R, III. (1997). Matrix-assisted laser desorption ionization/ quadrupole ion trap mass spectrometry of peptides: Application to the ...
... ion cyclotron resonance mass spectrometry. Anal. Chem. 71, 2076–2084. Jonscher, K. R., and Yates, J. R, III. (1997). Matrix-assisted laser desorption ionization/ quadrupole ion trap mass spectrometry of peptides: Application to the ...
Page 22
... ion trap mass spectrometry. Anal. Chem. 69, 4002–4009. Rodriguez, M. S., Desterro, J. M., Lain, S., Midgley, C. A., Lane, D. P., and Hay, R. T. (1999). SUMO-1 modification activates the transcriptional response of p53. EMBOJ. 18, 6455 ...
... ion trap mass spectrometry. Anal. Chem. 69, 4002–4009. Rodriguez, M. S., Desterro, J. M., Lain, S., Midgley, C. A., Lane, D. P., and Hay, R. T. (1999). SUMO-1 modification activates the transcriptional response of p53. EMBOJ. 18, 6455 ...
Page 32
... ions from large biological molecules, such as proteins, peptides, DNA, and RNA. The production of multiply charged ions makes the measurement of high molecular mass proteins amenable to instruments with limited m/z ranges, such as ion-trap ...
... ions from large biological molecules, such as proteins, peptides, DNA, and RNA. The production of multiply charged ions makes the measurement of high molecular mass proteins amenable to instruments with limited m/z ranges, such as ion-trap ...
Page 39
... ion selection and MS/MS capabilities of a triple quadrupole mass spectrometer with the high mass accuracy and ... Trap Mass Spectrometer The popularity of the quadrupole ion trap has its roots in the discovery and development of the mass ...
... ion selection and MS/MS capabilities of a triple quadrupole mass spectrometer with the high mass accuracy and ... Trap Mass Spectrometer The popularity of the quadrupole ion trap has its roots in the discovery and development of the mass ...
Contents
1 | |
25 | |
57 | |
85 | |
Current Strategies for Quantitative Proteomics | 133 |
Proteome Analysis of Posttranslational Modifications | 161 |
Mapping Protein Modifications with Liquid ChromatographyMass Spectrometry and the SALSA Algorithm | 195 |
Emerging Role of Mass Spectrometry in Structural and Functional Proteomics | 217 |
Application of Separation Technologies to Proteomics Research | 249 |
Proteomics of Membrane Proteins | 271 |
Proteomics in Drug Discovery | 309 |
Maximizing the Amount of Protein Samples for Structure Determination | 343 |
Proteomics and Bioinformatics | 353 |
AUTHOR INDEX | 371 |
SUBJECT INDEX | 403 |
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Proteome Characterization and Proteomics Timothy D. Veenstra,Richard D. Smith No preview available - 2003 |
Common terms and phrases
2D-PAGE abundance acid activity addition adducts affinity allows amino AMTs Anal analysis analyzed Anderson application approach Biochem Biol biological capillary cell changes characterization charged Chem chromatography combination compared complex containing corresponding database demonstrated described detected determined developed digestion disease drug effective Electrophoresis elution ESI-MS et al example expression extracted fractions fragmentation FTICR function gene genome glycosylation human identified increase indicated interactions ionization isolated isotopic labeling limited loss mapping Mass Spectrom mass spectrometry measurements membrane proteins methods mixture modifications molecular MS-MS MS/MS observed obtained organism pairs peptides phosphopeptides phosphorylation possible potential predicted present protein protein expression proteome proteome analysis quantitative range relative require residues SALSA sample selected sensitivity separation sequence shown signaling single specific spectra spectrum staining strategy structural studies tags tandem techniques trap tryptic two-dimensional
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Page 338 - Hunt, DF, Henderson, RA, Shabanowitz, J., Sakaguchi, K., Michel, H., Sevilir, N., Cox, AL, Appella, E., and Engelhard, VH Characterization of peptides bound to the class I MHC molecule HLA-A2.1 by mass spectrometry.
Page 191 - Brown, PO and Botstein, D. (1999) Exploring the new world of the genome with DNA microarrays.
Page 130 - Gygi, SP, Rist, B., Gerber, SA, Turecek, F., Gelb, MH, and Aebersold, R. (1999). Quantitative analysis of complex protein mixtures using isotope-coded affinity tags.
Page 335 - The potential use of laser capture microdissection to selectively obtain distinct populations of cells for proteomic analysis — preliminary findings. Electrophoresis, 20, 689-700 (2000).
Page 127 - Pacific Northwest Laboratory is operated by Battelle Memorial Institute for the US Department of Energy under Contract DE-AC06-76-RLO 1830.
Page 128 - Wilm, M., Shevchenko, A., Houthaeve, T., Breit, S., Schweigerer, L., Fotsis, T., and Mann, M. (1996). Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry.
Page 336 - An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database.