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Mass spectrometry peptides/proteins

Wienkoop, S., Glinski, M., Tanaka, N., Tolstikov, V.V., Fiehn, O., Weckwerth, W. (2004). Linking protein fractionation with multidimensional monolithic reversed-phase peptide chromatography/mass spectrometry enhances protein identification from complex mixtures even in the presence of abundant proteins. Rapid Commun. Mass Spectrom. 18, 643-650. [Pg.176]

Andersson M, Groseclose MR, Deutch AY, et al. Imaging mass spectrometry of proteins and peptides 3D volume reconstruction. Nat. Methods 2008 5 101-108. [Pg.397]

Kalkhof, S. et al. (2005a) Chemical cross-linking and high-performance fourier transform ion cyclotron resonance mass spectrometry for protein interaction analysis Application to a calmodulin/target peptide complex. Anal. Chem. 77, 495-503. [Pg.1080]

Cao P. and Moini M. (1998), Capillary electrophoresis/electrospray ionization high mass accuracy time-of-flight mass spectrometry for protein identification using peptide mapping, Rapid Commun. Mass Spectrom. 12, 864-870. [Pg.271]

Johnson R.S. and Taylor J.A. (2000), Searching sequence databases via de novo peptide sequencing by tandem mass spectrometry, in Methods in Molecular Biology, Vol. 146, Mass Spectrometry of Proteins and Peptides, pp. 41-61, Chapman J.R., Ed., Humana Press, Totowa, NJ. [Pg.272]

Mass Spectrometry of Proteins and Peptides Chapman, J.R., editor Humana Press 2000. [Pg.12]

Monton, M. R. N., and Terabe, S. (2005). Recent developments in capillary electrophoresis-mass spectrometry of proteins and peptides. Anal. Sci. 21, 5 — 13. [Pg.302]

Fig. 3A, B Strategies for the analysis of complex protein mixtures. A Proteins are separated by 2D PAGE and the relevant protein spots excised from the gel, digested, and analyzed by mass spectrometry. B Proteins are first digested into small peptides and then fractionated by two rounds of chromatography before each peptide is analyzed by mass spectrometry... Fig. 3A, B Strategies for the analysis of complex protein mixtures. A Proteins are separated by 2D PAGE and the relevant protein spots excised from the gel, digested, and analyzed by mass spectrometry. B Proteins are first digested into small peptides and then fractionated by two rounds of chromatography before each peptide is analyzed by mass spectrometry...
Griffiths, W.J. (2000). Nanospray mass spectrometry in protein and peptide chemistry. EXS, 88, 69-79. [Pg.175]

Jonsson, A.P. (2001). Mass spectrometry for protein and peptide characterisation. Cell. Mol. Life Scl, 58(7), 868-884. [Pg.176]

Humeny A, Kislinger T, Becker CM, Pischetsrieder M. Qualitative detennination of specific protein glycation products by matrix-assisted laser desorption/ionization mass spectrometry Peptide mapping. J Agric Food Client 2002 50(7) 2153—2160. [Pg.306]

The QMS platform combines the identification of proteins with their quantitative detection in one procedure. While protein identification can be deduced from peptide mass fingerprinting (PMF) or MS/MS spectra (see section Mass Spectrometry (MS)), protein quantitation is based on analysing either peak areas or signal intensities, or a combination of both. Several computer programs, in most cases reagent specific ones, are available. For each peak, quantitation values are calculated before differentially expressed proteins are identified by the comparison of control and treated samples. [Pg.866]

The methods for each study are divided into the initial protein separation step, a second separation step if applicable, the type of mass analysis, and the software used for peptide identification. ID = one dimensional polyacrylamide gel electrophoresis, 2D = two dimensional polyacrylamide gel electrophoresis, MS = mass spectrometry (peptide mass fingerprinting), MS/MS = tandem mass spectrometry, MALDI-TOF = matrix assisted laser desorption/ionization-time of flight, MS FIT = software from Protein Prospector, http //prospector.ucsf edu/, ESI = electrospray ionization, Q-TOF = quadrupole-time of flight, PPSS2 =Protana s Proteomic Software Suite (ProtanaEngineering, Odense, Denmark), Mascot = Matiix Science, http //www.matrixscience.com/, TOF-TOF = MALDI plus TOF tandem mass spectrometry, RP-HPLC = reverse phase high performance liquid chromatography, Q-IT = quadrupole ion trap, LIT = linear ion trap. Bioworks = Thermo Electron Corporation. [Pg.104]

Eckerskom, C., Stmpat, K., Kellermann, J., Lottspeich, F. and Hillenkamp, F. (1997) High-sensitivity peptide mapping by micro-LC with on-line membrane blotting and subsequent detection by scanning-IR-MALDI mass spectrometry. J. Protein Chem. 16, 349-362. [Pg.376]

D. Amott, J. Shabanowtiz, and D.F. Hunt. 1993. Mass spectrometry of proteins and peptides Sensitive and accurate mass measurement and sequence analysis Clin. Chem. 39 2005-2010. (PubMed)... [Pg.192]

MALDI-TOF Requires liigh resoludon mass spectrometry for protein identificadon based on peptide fmgerpimdng. Analydcal... [Pg.727]

MALDI-TOF Requires high resolution mass spectrometry for protein identification based on peptide fingerprinting. Analytical... [Pg.727]

Medzihradszky, K.F., H. Leffler, M.A. Baldwin and A. Burlinghame. Protein identification by in-gel digestion, high-performance liquid chromatography and mass spectrometry peptide analysis by complementary ionization techniques. J. Am. Soc. Mass Spectrom. 12 215-221, 2001. [Pg.114]

McMahon, G. Mass spectrometry peptides and proteins. Encyclopedia of Analytical Science (2nd ed), Eds P Worsfold, A Townshend and C Poole. ISBN 012764100-9. Elsevier, 501-509 (2005). [Pg.62]


See other pages where Mass spectrometry peptides/proteins is mentioned: [Pg.72]    [Pg.346]    [Pg.690]    [Pg.146]    [Pg.152]    [Pg.50]    [Pg.333]    [Pg.227]    [Pg.71]    [Pg.223]    [Pg.230]    [Pg.287]    [Pg.49]    [Pg.199]    [Pg.725]    [Pg.725]    [Pg.3048]    [Pg.110]    [Pg.87]    [Pg.145]    [Pg.375]   
See also in sourсe #XX -- [ Pg.266 , Pg.267 , Pg.268 ]




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