Multiplexed Post-Experimental Monoisotopic Mass Refinement (mPE-MMR) to Increase Sensitivity and Accuracy in Peptide Identifications from Tandem Mass Spectra of Cofragmentation
DC Field | Value | Language |
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dc.contributor.author | Madar, Inamul Hasan | - |
dc.contributor.author | Ko, Seung-Ik | - |
dc.contributor.author | Kim, Hokeun | - |
dc.contributor.author | Mun, Dong-Gi | - |
dc.contributor.author | Kim, Sangtae | - |
dc.contributor.author | Smith, Richard D. | - |
dc.contributor.author | Lee, Sang-Won | - |
dc.date.accessioned | 2021-09-03T10:51:10Z | - |
dc.date.available | 2021-09-03T10:51:10Z | - |
dc.date.created | 2021-06-16 | - |
dc.date.issued | 2017-01-17 | - |
dc.identifier.issn | 0003-2700 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/84901 | - |
dc.description.abstract | Mass spectrometry (MS)-based proteomics, which uses high-resolution hybrid mass spectrometers,such as the quadrupole-orbitrap mass spectrometer, can yield tens of thousands of tandem mass (MS/MS) spectra of high resolution dining a routine bottom-up experiment. Despite being a fundamental and key step in MS-based proteomics, the accurate determination and assignment of precursor monoisotopic masses to the MS/MS spectra remains difficult. The difficulties stem from imperfect isotopic envelopes of precursor ions, inaccurate charge states for precursor ions, and cofragmentation. We describe a composite method of utilizing MS data to assign accurate monoisotopic masses to MS/MS spectra, including those subject to cofragmentation. The method, "multiplexed post-experiment monoisotopic mass refinement" (mPE-MMR), consists of the following: multiplexing of precursor masses to assign multiple monoisotopic masses of cofragmented peptides to the corresponding multiplexed MS/MS spectra, multiplexing of charge states to assign correct charges to the precursor ions of MS/MS spectra with no charge information, and mass correction for inaccurate monoisotopic peak picking. When combined with MS-GF+, a database search algorithm based on fragment mass difference, mPE-MMR effectively increases both sensitivity and accuracy in peptide identification from complex high-throughput proteomics data compared to conventional-methods. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | AMER CHEMICAL SOC | - |
dc.subject | CHARGE-STATE DETERMINATION | - |
dc.subject | MIXTURE SPECTRA | - |
dc.subject | TOOL | - |
dc.subject | SPECTROMETRY | - |
dc.subject | MAXQUANT | - |
dc.title | Multiplexed Post-Experimental Monoisotopic Mass Refinement (mPE-MMR) to Increase Sensitivity and Accuracy in Peptide Identifications from Tandem Mass Spectra of Cofragmentation | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Lee, Sang-Won | - |
dc.identifier.doi | 10.1021/acs.analchem.6b03874 | - |
dc.identifier.scopusid | 2-s2.0-85035116865 | - |
dc.identifier.wosid | 000392458100031 | - |
dc.identifier.bibliographicCitation | ANALYTICAL CHEMISTRY, v.89, no.2, pp.1244 - 1253 | - |
dc.relation.isPartOf | ANALYTICAL CHEMISTRY | - |
dc.citation.title | ANALYTICAL CHEMISTRY | - |
dc.citation.volume | 89 | - |
dc.citation.number | 2 | - |
dc.citation.startPage | 1244 | - |
dc.citation.endPage | 1253 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Chemistry | - |
dc.relation.journalWebOfScienceCategory | Chemistry, Analytical | - |
dc.subject.keywordPlus | CHARGE-STATE DETERMINATION | - |
dc.subject.keywordPlus | MIXTURE SPECTRA | - |
dc.subject.keywordPlus | TOOL | - |
dc.subject.keywordPlus | SPECTROMETRY | - |
dc.subject.keywordPlus | MAXQUANT | - |
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