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.
|
From inside the book
Results 1-5 of 61
Page 9
... mass spectral analysis. The first strategy advocates the use of multidimensional separations so that the number of peptides analyzed by the mass spectrometer at any given time is minimized. The fewer the number of peptides within any ...
... mass spectral analysis. The first strategy advocates the use of multidimensional separations so that the number of peptides analyzed by the mass spectrometer at any given time is minimized. The fewer the number of peptides within any ...
Page 27
... mass spectrum of a protein's peptide fragments (typically produced by digestion with an enzyme with well-defined ... mass spectrum of a tryptic digest of an unknown protein. The measured masses are then compared with the theoretical ...
... mass spectrum of a protein's peptide fragments (typically produced by digestion with an enzyme with well-defined ... mass spectrum of a tryptic digest of an unknown protein. The measured masses are then compared with the theoretical ...
Page 28
... mass spectrum Theoretical tryptic peptides Protein sequence SEMHIKHYTTKILGFREE GDSCPLKQWDDSKILVA VADKLLEYEEKILLFNSA ... mass spectrometry. Bottom: In the database search, each protein sequence in the database is digested according to the ...
... mass spectrum Theoretical tryptic peptides Protein sequence SEMHIKHYTTKILGFREE GDSCPLKQWDDSKILVA VADKLLEYEEKILLFNSA ... mass spectrometry. Bottom: In the database search, each protein sequence in the database is digested according to the ...
Page 29
... mass spectrum of a tryptic digest of yeast enolase (46-kDa monomer). The protein is identified by comparing the observed masses with theoretical mass spectra generated from a virtual digestion of the proteins within the yeast protein or ...
... mass spectrum of a tryptic digest of yeast enolase (46-kDa monomer). The protein is identified by comparing the observed masses with theoretical mass spectra generated from a virtual digestion of the proteins within the yeast protein or ...
Page 30
... mass spectrum of the (M+H)+ ion at m/z 2442 of a tryptic digest of yeast enolase (46-kDa monomer). Mass spectrum was acquired with a QSTAR Pulsar mass spectrometer (Applied Biosystems, Foster City, CA), MS/MS sequencing indicates that ...
... mass spectrum of the (M+H)+ ion at m/z 2442 of a tryptic digest of yeast enolase (46-kDa monomer). Mass spectrum was acquired with a QSTAR Pulsar mass spectrometer (Applied Biosystems, Foster City, CA), MS/MS sequencing indicates that ...
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 |
Other editions - View all
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
Popular passages
Page 23 - D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern...
Page 18 - Alizadeh AA, Eisen MB, Davis RE, Ma C, Lossos IS, Rosenwald A, Boldrick JC, Sabet H, Tran T, Yu X, Powell JI, Yang L, Marti GE, Moore T, Hudson...
Page 19 - Bittner M, Meltzer P, Chen Y, Jiang Y, Seftor E. Hendrix M. Radmacher M, Simon R. Yakhini Z, Ben-Dor A, Sampas N, Dougherty E. Wang E. Marincola F. Gooden C. Lueders J. Glatfelter A, Pollock P, Carpten J, Gillanders E, Leja D. Dietrich K, Beaudry C. Berens M, Alberts D. Sondak V.
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.