Correction of translational start site by identification of N-terminal peptide. Correction of translational start site by identification of N-terminal.

Slides:



Advertisements
Similar presentations
binding sites 58 of the 473 unambiguously assigned phosphorylation sites are predicted by Scansite to be sites for binding. 50 of these correspond.
Advertisements

Sequence alignment of C-terminal phosphorylated plant aquaporins
Phosphopeptide sequencing by MALDI-TOF/TOF of the C-terminal tail of AtPIP2;1.A, MS/MS spectrum of singly phosphorylated 277SLGSFRSAANV287 (m/z ).
Distribution of disorder in the cytosolic phosphoproteome
Phosphorylation and sequence disorder in microtubule-associated protein Tau.A, schematic illustration of the domain profile of Tau with all known phosphorylation.
Distribution of phosphorylation sites identified in the cytosolic phosphoproteome.A, numbers of approved phosphopeptides, previously phosphorylated peptides,
Phosphopeptide sequencing by MALDI-TOF/TOF of the C-terminal tail of AtPIP2;4.A, MS/MS spectrum of singly phosphorylated 277ALGSFGSFGSFRSFA291 (m/z ).
Phosphopeptide sequencing by MALDI-TOF/TOF of the C-terminal tail of AtPIP2;7.A, MS/MS spectrum of singly phosphorylated 270ALGSFRSNATN280 (m/z ).
Phosphopeptides identified harboring minimal binding motifs
Percentage of proteins identified in envelope membrane extracts according to the purification method and the number of transmembrane domains. Percentage.
Novel phosphorylation sites on H+-ATPase proteins
A, high resolution MS/MS spectrum (lower panel) of 1435
Frequency distribution of the GRAVY of the theoretical proteins (open bars) and of 110 genes encoding proteins identified on a 2-D electrophoresis gel,
Complementary identification and novel protein discovery
Protein information in the Human Protein Atlas.
Top-down protein identification.
Distributions of the ELDP values and Mascot scores for all protein identifications.a, frequency of ELDP value returned by correct (gray bars) and incorrect.
Significantly enriched phosphorylation motifs from up-regulated phosphopeptides by Motif-X analysis. Significantly enriched phosphorylation motifs from.
Visual validation of the computational outputs.
Epitope Mapping Performance using a single peptide microarray.
Schematic representation of proteogenomic annotation strategy.
Novel p53 target genes identified by RNA-Seq, pSILAC and ChIP-Seq.
A, Averaged full MS (ions converted to monoisotopic MW by Xcalibur Xtract) of Segment I-3 (see supplemental Fig. A, Averaged full MS (ions converted to.
Bottom-up proteomic characterization of MALDI IMS samples.
A, Base peak chromatogram of apomyoglobin digest generated by 0
Colonopshere-enriched proteins display functional interactions.
Identification of SUMO3peptides from 2D-LC-MS/MS analyses of a tryptic digest of HEK293-SUMO3 cells using DDA and DIA methods. Identification of SUMO3peptides.
Proteins previously reported in published MALDI IMS studies and their frequency of observation in the present study. Proteins previously reported in published.
High correlation of expression changes of NMD-regulated genes identified by both the pSILAC screen and previously reported global RNA screens after UPF1.
N-terminal extension of a gene using peptides mapping upstream to an annotated start site. N-terminal extension of a gene using peptides mapping upstream.
Analysis of newly synthesized proteins by combined pulsed SILAC and click chemistry enrichment. Analysis of newly synthesized proteins by combined pulsed.
Schematic summarizing the various functions and features of MASH Suite Pro. Schematic summarizing the various functions and features of MASH Suite Pro.
Cleavage and splicing in a representative specific substrate sequence by yeast active site β subunits. Cleavage and splicing in a representative specific.
MS/MS spectra of INEILSNALKR with a Lys residue modified with SUMO1 or SUMO3 remnant chains. MS/MS spectra of INEILSNALKR with a Lys residue modified with.
Manual assessment of the quality of peptide spectra with scores ranging from 5 to 10 of OFFGEL electrophoresis fractions 3 and 4 that were rejected by.
Testing the effectiveness of the three-step peptide fractionation method.A, μLC mass chromatograms of SCX fractions for an acidic FFE fraction. Testing.
Altered pathways in prostate cancer.
Resolution and mass accuracy of A, a peptide isotope cluster (m/z 558
Interaction networks of the regulated phosphoproteins.
LC-MS/MS analyses of synthetic peptides with SUMO1 and SUMO3 remnant chains using ETD, CID, and HCD activation modes. LC-MS/MS analyses of synthetic peptides.
2D-LC-MS/MS analysis of tryptic digest of HEK293-SUMO3 cells (2 μg inj
The PPAR-α agonist GW7647 reduces experimentally induced myopia.
Identification of chaperonin GroEL (Rv0440) with representative MS/MS spectrum. Identification of chaperonin GroEL (Rv0440) with representative MS/MS spectrum.A,
Example of MS/MS spectrum of peptide FPTLTGFNR (hypothetical protein with signal peptide EAK88888; N77) from a protein digestion mixture prepared by labeling.
Plot of the deviation of the predicted pI value of every peptide spectrum from the average pI calculated for each fraction for validated (a) and non-validated.
Relative quantification of cis and trans PSP gp10040–42/47–52 variants
Distribution of the phosphoproteins based on GO analysis, including biological process (Left) and cellular component (Right). Distribution of the phosphoproteins.
A, Absolute ion intensities of m/z 322, 922 and 1522 as function of the transfer time. A, Absolute ion intensities of m/z 322, 922 and 1522 as function.
K-Means clustering of protein and mRNA expression patterns after PPAR agonists treatments. k-Means clustering of protein and mRNA expression patterns after.
Comparison of mapped epitopes and peptides identified in immuno-SILAC screening of polyclonal antibodies against trypsin-digested PrESTs. Comparison of.
Number of genes/antibodies included in the database.
Bar plot representation of the transcriptomic changes in Δsaci_ptp and Δsaci_pp2a. Bar plot representation of the transcriptomic changes in Δsaci_ptp and.
Analytical metrics of yeast proteome analysis using the Q-OT-qIT (Fusion) as compared with qIT-OT (Orbitrap Elite) and Q-OT (Q-Exactive) hybrids. Analytical.
Biochemical characterization of the protein phosphatases Saci-PP2A.
Analysis of a tryptic digest of subunit B12 by MALDI-TOF mass spectrometry. Analysis of a tryptic digest of subunit B12 by MALDI-TOF mass spectrometry.
Biochemical characterization of the protein phosphatases Saci-PTP.
Identification and quantification of cathepsin D in chronic pancreatitis.A, identification of two peptides, AIGAVPLIQGEYMIPCEK (A) and LLDIACWIHH (MS/MS.
Voronoi treemaps (109) comparing protein expression profiles of M
Illustration of chromatography metric C-2A applied to LC-MS/MS data from three Thermo LTQ systems in analyses of yeast proteome samples in CPTAC Study.
Classification of the 1458 identified proteins into molecular functions. Classification of the 1458 identified proteins into molecular functions. The pie.
Separation of colonospheres from differentiated tumor cells by cluster analysis. Separation of colonospheres from differentiated tumor cells by cluster.
Expression of σ in SCCs Expression of σ in SCCs. Shown is a magnified section of a representative 2D PAGE gel run with a lysate from an SCC.
Proteomics analysis of NaPi-IIa C terminus binding to PDZ proteins.
Schematic of AIMS-to-MRM experiment.
GeneGoTM-based signaling pathway annotations of proteins identified in CD56+ NK cell subsets. GeneGoTM-based signaling pathway annotations of proteins.
Changes in protein expression during distinct stages of NK cell differentiation. Changes in protein expression during distinct stages of NK cell differentiation.
Phosphopeptides identified harboring minimal binding motifs
Survey of phosphorylation motifs
MS3 for peptide identification and mapping phosphorylation sites
Model of the change in receptor structure on engagement of the ligand IFN-γ. Model of the change in receptor structure on engagement of the ligand IFN-γ.
Presentation transcript:

Correction of translational start site by identification of N-terminal peptide. Correction of translational start site by identification of N-terminal peptide.A, A Peptide GDASLTTELGR with a nontryptic N terminus was mapped downstream of the annotated translational start site of the gene Rv1106c. Gene model by Gene prediction program FgeneSB and orthologous protein from M. tuberculosis Sumu004 support the re-annotation of the TSS by shortening protein length by 4 amino acids. B, Protein sequence of Rv1106c is shown. Text in gray indicates amino acids removed in the revised gene model for Rv1106c. C, A representative MS/MS spectrum for the peptide GDASLTTELGR is shown. Dhanashree S. Kelkar et al. Mol Cell Proteomics 2011;10:M111.011627 © 2011 by The American Society for Biochemistry and Molecular Biology, Inc.