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Bovine alpha-lactalbumine microLC-timsTOF PRo

ABSTRACT: The investigation focused on the impact of software settings Bovine alpha-lactalbumin was used as a model protein due to its relatively small size, allowing for detailed tracking of any resulting changes. Furthermore, the reproducibility of results was investigated based on 18 measurements of the same sample.

INSTRUMENT(S): timsTOF Pro

ORGANISM(S): Bos Taurus (bovine)

TISSUE(S): Milk

SUBMITTER: Andreas Mauser

LAB HEAD: Monika Pischetsrieder

PROVIDER: PXD050363 | Pride | 2024-09-23

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	ALA_Reproducibility.zip	Other
	ALA_Reproducibility_PEAKS-Studio.zip	Other
	Untreated-ALA_Sequenze-coverage.zip	Other
	Untreated-ALA_Sequenze-coverage_PEAKS-Studio.zip	Other
	heated_lactose-modified_untreated_ALA_enzyme-settings.rar	Other

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Publications

Influence of Software Settings on the Identification Rate, Quantification Results, and Reproducibility in Profiling Post-Translational Modifications by Microflow Liquid Chromatography-Ion Mobility-Quadrupole Time-Of-Flight Analysis Using PEAKS Software.

Mauser Andreas A Gensberger-Reigl Sabrina S Dalabasmaz Sevim S Schichtl Theresa Maria TM Dittrich Daniel D Pischetsrieder Monika M

Journal of proteome research 20240916

The influence of data evaluation parameters on qualitative and quantitative results of untargeted shotgun profiling of enzymatic and nonenzymatic post-translational modifications (PTMs) was investigated in a model of bovine whey protein α-lactalbumin heated with lactose. Based on the same raw data, individual adjustments to the protein database and enzyme settings of PEAKS studio software increased the identification rate from 27 unmodified peptides to 48 and from 322 peptides in total to 535. T ...[more]

PMID: 39284794

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Proteomic Analysis of Tears and Conjunctival Cells Collected with Schirmer Strips Using timsTOF Pro: Preanalytical Considerations.

Project description:This study aimed to investigate the human proteome profile of samples collected from whole (W) Schirmer strips (ScS) and their two parts-the bulb (B) and the rest of the strip (R)-with a comprehensive proteomic approach using a trapped ion mobility mass spectrometer, the timsTOF Pro. Eight ScS were collected from two healthy subjects at four different visits to be separated into three batches, i.e., 4W, 4B, and 4R. In total, 1582 proteins were identified in the W, B, and R batches. Among all identified proteins, binding proteins (43.4%) and those with catalytic activity (42.2%) constituted more than 80% of the molecular functions. The most represented biological processes were cellular processes (31.2%), metabolic processes (20.8%), and biological regulation (13.1%). Enzymes were the most represented protein class (41%), consisting mainly of hydrolases (47.5%), oxidoreductases (22.1%), and transferases (16.7%). The bulb (B), which is in contact with the conjunctiva, might collect both tear and cell proteins and therefore promote the identification of more proteins. Processing B and R separately before mass spectrometry (MS) analysis, combined with the high data acquisition speed and the addition of ion-mobility-based separation in the timsTOF Pro, can bring a new dimension to biomarker investigations of a limited sample such as tear fluid.

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LC-MS/MS interactomics analysis of Praf2 with timsTOF Pro

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Proteomics Tool Spike-in dataset analyzed on a timsTOF Pro

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