Proteomics

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Protein-protein interactions of PID-3 in C. briggsae


ABSTRACT: A mass spectrometry-based label-free proteomics analysis was performed to study the protein binders of PID-3 in C. briggsae. Anti-PID-3 and IgG control pull-downs were performed on C. briggsae. Proteins were digested in-gel by trypsin. Peptides were measured on a Q Exactive Plus Orbitrap mass spectrometer. Raw data files were processed by MaxQuant software package (version 2.1.3.0) using its integrated Andromeda search engine. Spectral data were searched against a target-decoy database consisting of the forward and reverse sequences of the UniProt C. briggsae (release 2023_02; 21,756 entries) and E. coli (release 2023_01; 5,064 entries) reference proteomes and a list of common contaminants. False discovery rate (FDR) was set to 1% at both peptide and protein levels. MaxLFQ quantification algorithm was employed.

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Caenorhabditis Briggsae (ncbitaxon:6238)

SUBMITTER: Rene Ketting  

PROVIDER: MSV000099274 | MassIVE |

SECONDARY ACCESSION(S): PXD068824

REPOSITORIES: MassIVE

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