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CharmeRT - CharmeRT: Boosting peptide identifications by chimeric spectra identification and retention time prediction

ABSTRACT: Files include several HeLa tryptic digests with different isolation widths and different gradient times for chimeric spectra identification and validation, each of them as three technical replicates

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Hela Cell

SUBMITTER: Viktoria Dorfer

LAB HEAD: Karl Mechtler

PROVIDER: PXD007750 | Pride | 2018-06-12

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	HeLa_100ng_isow2_3hgradient_datasetI_rep1.msf	Msf
	HeLa_100ng_isow2_3hgradient_datasetI_rep1.raw	Raw
	HeLa_100ng_isow2_3hgradient_datasetI_rep2.msf	Msf
	HeLa_100ng_isow2_3hgradient_datasetI_rep2.raw	Raw
	HeLa_100ng_isow2_3hgradient_datasetI_rep3.msf	Msf

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Publications

CharmeRT: Boosting Peptide Identifications by Chimeric Spectra Identification and Retention Time Prediction.

Dorfer Viktoria V Maltsev Sergey S Winkler Stephan S Mechtler Karl K

Journal of proteome research 20180628 8

Coeluting peptides are still a major challenge for the identification and validation of MS/MS spectra, but carry great potential. To tackle these problems, we have developed the here presented CharmeRT workflow, combining a chimeric spectra identification strategy implemented as part of the MS Amanda algorithm with the validation system Elutator, which incorporates a highly accurate retention time prediction algorithm. For high-resolution data sets this workflow identifies 38-64% chimeric spectr ...[more]

PMID: 29863353

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