Proteomics

Dataset Information

0

PROCAL: A set of 40 peptide standards for retention time indexing, column performance monitoring and collision energy calibration

ABSTRACT: We describe PROCAL (ProteomeTools Standard), a set of 40 synthetic peptides that span the entire hydrophobicity range of tryptic digests, enabling not only accurate determination of retention time indices but also monitoring of chromatographic separation performance over time. The fragmentation characteristics of the peptides can also be used to calibrate and compare collision energies between mass spectrometers. The sequences of all selected peptides do not occur in any natural protein, thus eliminating the need for stable isotope labeling and allowing straightforward integration into standard peptide identification strategies employing database searching or spectral library matching.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Artificial Sequences

SUBMITTER: Daniel Zolg  

LAB HEAD: Bernhard Kuster

PROVIDER: PXD006832 | Pride | 2017-09-07

REPOSITORIES: Pride

Json Xml

Dataset's files

Source:
Action DRS
Fic2b_170329_PROST_200fmol_4to42_R1.raw Raw
Fig1a_160909_PROST_100fmol_60min_4to42_R1.raw Raw
Fig1b_160914_PROST_Hela_500ng_100fmol_60min_4to42_R1.raw Raw
Fig1b_SEARCH.zip Other
Fig1c_160824_PROST_200fmol_120min_4to32_R1.raw Raw
Items per page:
1 - 5 of 43
altmetric image

Publications

PROCAL: A Set of 40 Peptide Standards for Retention Time Indexing, Column Performance Monitoring, and Collision Energy Calibration.

Zolg Daniel Paul DP   Wilhelm Mathias M   Yu Peng P   Knaute Tobias T   Zerweck Johannes J   Wenschuh Holger H   Reimer Ulf U   Schnatbaum Karsten K   Kuster Bernhard B  

Proteomics 20171024 21

Beyond specific applications, such as the relative or absolute quantification of peptides in targeted proteomic experiments, synthetic spike-in peptides are not yet systematically used as internal standards in bottom-up proteomics. A number of retention time standards have been reported that enable chromatographic aligning of multiple LC-MS/MS experiments. However, only few peptides are typically included in such sets limiting the analytical parameters that can be monitored. Here, we describe PR  ...[more]

Similar Datasets

Proteomics Peptide collision cross section of 22 post-translational modifications
2023-08-25 | PXD042416 | Pride
Proteomics Partial covariance two-dimensional mass spectrometry for bio-molecular primary structure
2023-09-30 | PXD010631 | Pride
Proteomics Absolute Quantification of Yeast Proteins Using Synthetic Peptide Standards and TMT labeling
2020-03-13 | PXD015025 | Pride
Proteomics Quantification of H3K27 methylation using heavy peptides as standards
2020-04-23 | PXD018321 | Pride
Proteomics A Novel Two-Stage Tandem Mass Spectrometry Approach and Scoring Scheme for the Identification of O-GlcNAc Modified Peptides
2018-06-18 | PXD010152 | Pride
Proteomics A multi-omics dataset of human transcriptome and proteome stable reference
2023-07-11 | PXD043389 | Pride
Proteomics Chemical phosphoproteomic approaches reveal substrate specificity of phosphoprotein phosphatases-1 and -2
2020-07-14 | PXD013775 | Pride
Proteomics FastCAT accelerates absolute quantification of proteins by using multiple short non-purified chimeric standards
2022-04-01 | PXD030728 | Pride
Genomic Antigen Discovery in Melanoma
| phs001005 | dbGaP
Proteomics Standard Pressure LC-MS/MS Using 1.9um C18 Particles Column at Room Temperature
2022-02-28 | PXD002895 | Pride