Thorough Performance Evaluation of 213 nm Ultraviolet Photodissociation for Top-down Proteomics
We benchmarked ultraviolet photodissociation (UVPD) based on 213 nm photons for the characterization of proteoforms
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| Veröffentlicht in: | Molecular & cellular proteomics 2020-02, Vol.19 (2), p.405-420 |
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| creator | Fornelli, Luca Srzentić, Kristina Toby, Timothy K. Doubleday, Peter F. Huguet, Romain Mullen, Christopher Melani, Rafael D. dos Santos Seckler, Henrique DeHart, Caroline J. Weisbrod, Chad R. Durbin, Kenneth R. Greer, Joseph B. Early, Bryan P. Fellers, Ryan T. Zabrouskov, Vlad Thomas, Paul M. Compton, Philip D. Kelleher, Neil L. |
| description | We benchmarked ultraviolet photodissociation (UVPD) based on 213 nm photons for the characterization of proteoforms |
| doi_str_mv | 10.1074/mcp.TIR119.001638 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_7000117</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S1535947620350878</els_id><sourcerecordid>2331632399</sourcerecordid><originalsourceid>FETCH-LOGICAL-c451t-8c0b0e97bc9d21e3b0659b695f48d1bd976e878ce82cc5025d0abdddea84b98e3</originalsourceid><addsrcrecordid>eNp9kU9r3DAQxUVJaf60H6CXomMu3kiWZUsUAiGkSSDQpWzOQpbGWRXbs5XsDf32VXC6pJeeNKD33gzvR8hnzlacNdXF4Harzf0PzvWKMV4L9Y6ccClkoStVHR3mpj4mpyn9ZKxkvJEfyLHgSildyxNiNluMOD9t6Rpih3GwowN6s7f9bKeAI8WOllzQcaCP_RTtPmAPE11vcUIfUkIXFl320g3uCo_PI11HnACH4NJH8r6zfYJPr-8Zefx2s7m-Kx6-395fXz0UrpJ8KpRjLQPdtE77koNoWS11W2vZVcrz1uumBtUoB6p0TrJSemZb7z1YVbVagTgjl0vubm4H8A7GfGxvdjEMNv42aIP592cMW_OEe9OwXB1vcsD5a0DEXzOkyQwhOeh7OwLOyZRC5IZLoXWW8kXqIqYUoTus4cy8gDEZjFnAmAVM9nx5e9_B8ZdEFnxdBJBb2geIJrkAGYYPEdxkPIb_xP8BVIGhLw</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2331632399</pqid></control><display><type>article</type><title>Thorough Performance Evaluation of 213 nm Ultraviolet Photodissociation for Top-down Proteomics</title><source>MEDLINE</source><source>EZB-FREE-00999 freely available EZB journals</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><source>Free Full-Text Journals in Chemistry</source><creator>Fornelli, Luca ; Srzentić, Kristina ; Toby, Timothy K. ; Doubleday, Peter F. ; Huguet, Romain ; Mullen, Christopher ; Melani, Rafael D. ; dos Santos Seckler, Henrique ; DeHart, Caroline J. ; Weisbrod, Chad R. ; Durbin, Kenneth R. ; Greer, Joseph B. ; Early, Bryan P. ; Fellers, Ryan T. ; Zabrouskov, Vlad ; Thomas, Paul M. ; Compton, Philip D. ; Kelleher, Neil L.</creator><creatorcontrib>Fornelli, Luca ; Srzentić, Kristina ; Toby, Timothy K. ; Doubleday, Peter F. ; Huguet, Romain ; Mullen, Christopher ; Melani, Rafael D. ; dos Santos Seckler, Henrique ; DeHart, Caroline J. ; Weisbrod, Chad R. ; Durbin, Kenneth R. ; Greer, Joseph B. ; Early, Bryan P. ; Fellers, Ryan T. ; Zabrouskov, Vlad ; Thomas, Paul M. ; Compton, Philip D. ; Kelleher, Neil L.</creatorcontrib><description>We benchmarked ultraviolet photodissociation (UVPD) based on 213 nm photons for the characterization of proteoforms <30 kDa from three different samples (Pseudomonas aeruginosa, mouse hearts and human fibroblasts). Product ion abundance analysis of 213 nm UVPD data sets was used for improving the database search ultimately leading to increased identification rates. 213 nm UVPD outperformed HCD in terms of proteoform characterization (defined by the C-score). Finally, we described UVPD fragmentation propensities and the observation of a 213 nm UVPD-specific product ion.
[Display omitted]
Highlights
•Analysis of product ions produced by 213 nm UVPD is used to refine database search.•A product ion at the N-terminus of Pro, y-2, is observed in 213 nm UVPD spectra.•213 nm UVPD provides more complete proteoform characterization than HCD.•HCD and 213 nm UVPD are complementary fragmentation methods for proteoforms <30 kDa.
Top-down proteomics studies intact proteoform mixtures and offers important advantages over more common bottom-up proteomics technologies, as it avoids the protein inference problem. However, achieving complete molecular characterization of investigated proteoforms using existing technologies remains a fundamental challenge for top-down proteomics. Here, we benchmark the performance of ultraviolet photodissociation (UVPD) using 213 nm photons generated by a solid-state laser applied to the study of intact proteoforms from three organisms. Notably, the described UVPD setup applies multiple laser pulses to induce ion dissociation, and this feature can be used to optimize the fragmentation outcome based on the molecular weight of the analyzed biomolecule. When applied to complex proteoform mixtures in high-throughput top-down proteomics, 213 nm UVPD demonstrated a high degree of complementarity with the most employed fragmentation method in proteomics studies, higher-energy collisional dissociation (HCD). UVPD at 213 nm offered higher average proteoform sequence coverage and degree of proteoform characterization (including localization of post-translational modifications) than HCD. However, previous studies have shown limitations in applying database search strategies developed for HCD fragmentation to UVPD spectra which contains up to nine fragment ion types. We therefore performed an analysis of the different UVPD product ion type frequencies. From these data, we developed an ad hoc fragment matching strategy and determined the influence of each possible ion type on search outcomes. By paring down the number of ion types considered in high-throughput UVPD searches from all types down to the four most abundant, we were ultimately able to achieve deeper proteome characterization with UVPD. Lastly, our detailed product ion analysis also revealed UVPD cleavage propensities and determined the presence of a product ion produced specifically by 213 nm photons. All together, these observations could be used to better elucidate UVPD dissociation mechanisms and improve the utility of the technique for proteomic applications.</description><identifier>ISSN: 1535-9476</identifier><identifier>EISSN: 1535-9484</identifier><identifier>DOI: 10.1074/mcp.TIR119.001638</identifier><identifier>PMID: 31888965</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Carbonic Anhydrases ; Cells, Cultured ; Chromatography, Liquid ; FDR ; Fibroblasts ; Fourier transform MS ; Fungal Proteins ; Humans ; mass spectrometry ; Mice ; Myocytes, Cardiac ; Myoglobin ; Photons ; post-translational modifications ; product ion ; protein identification ; proteoform ; Proteomics - methods ; Pseudomonas aeruginosa ; Tandem Mass Spectrometry ; Technological Innovation and Resources ; top-down proteomics ; Ubiquitin ; Ultraviolet Rays ; UVPD</subject><ispartof>Molecular & cellular proteomics, 2020-02, Vol.19 (2), p.405-420</ispartof><rights>2020 © 2020 Fornelli et al.</rights><rights>2020 Fornelli et al.</rights><rights>2020 Fornelli et al. 2020 Fornelli et al.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c451t-8c0b0e97bc9d21e3b0659b695f48d1bd976e878ce82cc5025d0abdddea84b98e3</citedby><cites>FETCH-LOGICAL-c451t-8c0b0e97bc9d21e3b0659b695f48d1bd976e878ce82cc5025d0abdddea84b98e3</cites><orcidid>0000-0001-6334-1046 ; 0000-0002-8815-3372 ; 0000-0003-2887-4765</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7000117/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7000117/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27923,27924,53790,53792</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31888965$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fornelli, Luca</creatorcontrib><creatorcontrib>Srzentić, Kristina</creatorcontrib><creatorcontrib>Toby, Timothy K.</creatorcontrib><creatorcontrib>Doubleday, Peter F.</creatorcontrib><creatorcontrib>Huguet, Romain</creatorcontrib><creatorcontrib>Mullen, Christopher</creatorcontrib><creatorcontrib>Melani, Rafael D.</creatorcontrib><creatorcontrib>dos Santos Seckler, Henrique</creatorcontrib><creatorcontrib>DeHart, Caroline J.</creatorcontrib><creatorcontrib>Weisbrod, Chad R.</creatorcontrib><creatorcontrib>Durbin, Kenneth R.</creatorcontrib><creatorcontrib>Greer, Joseph B.</creatorcontrib><creatorcontrib>Early, Bryan P.</creatorcontrib><creatorcontrib>Fellers, Ryan T.</creatorcontrib><creatorcontrib>Zabrouskov, Vlad</creatorcontrib><creatorcontrib>Thomas, Paul M.</creatorcontrib><creatorcontrib>Compton, Philip D.</creatorcontrib><creatorcontrib>Kelleher, Neil L.</creatorcontrib><title>Thorough Performance Evaluation of 213 nm Ultraviolet Photodissociation for Top-down Proteomics</title><title>Molecular & cellular proteomics</title><addtitle>Mol Cell Proteomics</addtitle><description>We benchmarked ultraviolet photodissociation (UVPD) based on 213 nm photons for the characterization of proteoforms <30 kDa from three different samples (Pseudomonas aeruginosa, mouse hearts and human fibroblasts). Product ion abundance analysis of 213 nm UVPD data sets was used for improving the database search ultimately leading to increased identification rates. 213 nm UVPD outperformed HCD in terms of proteoform characterization (defined by the C-score). Finally, we described UVPD fragmentation propensities and the observation of a 213 nm UVPD-specific product ion.
[Display omitted]
Highlights
•Analysis of product ions produced by 213 nm UVPD is used to refine database search.•A product ion at the N-terminus of Pro, y-2, is observed in 213 nm UVPD spectra.•213 nm UVPD provides more complete proteoform characterization than HCD.•HCD and 213 nm UVPD are complementary fragmentation methods for proteoforms <30 kDa.
Top-down proteomics studies intact proteoform mixtures and offers important advantages over more common bottom-up proteomics technologies, as it avoids the protein inference problem. However, achieving complete molecular characterization of investigated proteoforms using existing technologies remains a fundamental challenge for top-down proteomics. Here, we benchmark the performance of ultraviolet photodissociation (UVPD) using 213 nm photons generated by a solid-state laser applied to the study of intact proteoforms from three organisms. Notably, the described UVPD setup applies multiple laser pulses to induce ion dissociation, and this feature can be used to optimize the fragmentation outcome based on the molecular weight of the analyzed biomolecule. When applied to complex proteoform mixtures in high-throughput top-down proteomics, 213 nm UVPD demonstrated a high degree of complementarity with the most employed fragmentation method in proteomics studies, higher-energy collisional dissociation (HCD). UVPD at 213 nm offered higher average proteoform sequence coverage and degree of proteoform characterization (including localization of post-translational modifications) than HCD. However, previous studies have shown limitations in applying database search strategies developed for HCD fragmentation to UVPD spectra which contains up to nine fragment ion types. We therefore performed an analysis of the different UVPD product ion type frequencies. From these data, we developed an ad hoc fragment matching strategy and determined the influence of each possible ion type on search outcomes. By paring down the number of ion types considered in high-throughput UVPD searches from all types down to the four most abundant, we were ultimately able to achieve deeper proteome characterization with UVPD. Lastly, our detailed product ion analysis also revealed UVPD cleavage propensities and determined the presence of a product ion produced specifically by 213 nm photons. All together, these observations could be used to better elucidate UVPD dissociation mechanisms and improve the utility of the technique for proteomic applications.</description><subject>Animals</subject><subject>Carbonic Anhydrases</subject><subject>Cells, Cultured</subject><subject>Chromatography, Liquid</subject><subject>FDR</subject><subject>Fibroblasts</subject><subject>Fourier transform MS</subject><subject>Fungal Proteins</subject><subject>Humans</subject><subject>mass spectrometry</subject><subject>Mice</subject><subject>Myocytes, Cardiac</subject><subject>Myoglobin</subject><subject>Photons</subject><subject>post-translational modifications</subject><subject>product ion</subject><subject>protein identification</subject><subject>proteoform</subject><subject>Proteomics - methods</subject><subject>Pseudomonas aeruginosa</subject><subject>Tandem Mass Spectrometry</subject><subject>Technological Innovation and Resources</subject><subject>top-down proteomics</subject><subject>Ubiquitin</subject><subject>Ultraviolet Rays</subject><subject>UVPD</subject><issn>1535-9476</issn><issn>1535-9484</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kU9r3DAQxUVJaf60H6CXomMu3kiWZUsUAiGkSSDQpWzOQpbGWRXbs5XsDf32VXC6pJeeNKD33gzvR8hnzlacNdXF4Harzf0PzvWKMV4L9Y6ccClkoStVHR3mpj4mpyn9ZKxkvJEfyLHgSildyxNiNluMOD9t6Rpih3GwowN6s7f9bKeAI8WOllzQcaCP_RTtPmAPE11vcUIfUkIXFl320g3uCo_PI11HnACH4NJH8r6zfYJPr-8Zefx2s7m-Kx6-395fXz0UrpJ8KpRjLQPdtE77koNoWS11W2vZVcrz1uumBtUoB6p0TrJSemZb7z1YVbVagTgjl0vubm4H8A7GfGxvdjEMNv42aIP592cMW_OEe9OwXB1vcsD5a0DEXzOkyQwhOeh7OwLOyZRC5IZLoXWW8kXqIqYUoTus4cy8gDEZjFnAmAVM9nx5e9_B8ZdEFnxdBJBb2geIJrkAGYYPEdxkPIb_xP8BVIGhLw</recordid><startdate>20200201</startdate><enddate>20200201</enddate><creator>Fornelli, Luca</creator><creator>Srzentić, Kristina</creator><creator>Toby, Timothy K.</creator><creator>Doubleday, Peter F.</creator><creator>Huguet, Romain</creator><creator>Mullen, Christopher</creator><creator>Melani, Rafael D.</creator><creator>dos Santos Seckler, Henrique</creator><creator>DeHart, Caroline J.</creator><creator>Weisbrod, Chad R.</creator><creator>Durbin, Kenneth R.</creator><creator>Greer, Joseph B.</creator><creator>Early, Bryan P.</creator><creator>Fellers, Ryan T.</creator><creator>Zabrouskov, Vlad</creator><creator>Thomas, Paul M.</creator><creator>Compton, Philip D.</creator><creator>Kelleher, Neil L.</creator><general>Elsevier Inc</general><general>The American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0001-6334-1046</orcidid><orcidid>https://orcid.org/0000-0002-8815-3372</orcidid><orcidid>https://orcid.org/0000-0003-2887-4765</orcidid></search><sort><creationdate>20200201</creationdate><title>Thorough Performance Evaluation of 213 nm Ultraviolet Photodissociation for Top-down Proteomics</title><author>Fornelli, Luca ; Srzentić, Kristina ; Toby, Timothy K. ; Doubleday, Peter F. ; Huguet, Romain ; Mullen, Christopher ; Melani, Rafael D. ; dos Santos Seckler, Henrique ; DeHart, Caroline J. ; Weisbrod, Chad R. ; Durbin, Kenneth R. ; Greer, Joseph B. ; Early, Bryan P. ; Fellers, Ryan T. ; Zabrouskov, Vlad ; Thomas, Paul M. ; Compton, Philip D. ; Kelleher, Neil L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c451t-8c0b0e97bc9d21e3b0659b695f48d1bd976e878ce82cc5025d0abdddea84b98e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Animals</topic><topic>Carbonic Anhydrases</topic><topic>Cells, Cultured</topic><topic>Chromatography, Liquid</topic><topic>FDR</topic><topic>Fibroblasts</topic><topic>Fourier transform MS</topic><topic>Fungal Proteins</topic><topic>Humans</topic><topic>mass spectrometry</topic><topic>Mice</topic><topic>Myocytes, Cardiac</topic><topic>Myoglobin</topic><topic>Photons</topic><topic>post-translational modifications</topic><topic>product ion</topic><topic>protein identification</topic><topic>proteoform</topic><topic>Proteomics - methods</topic><topic>Pseudomonas aeruginosa</topic><topic>Tandem Mass Spectrometry</topic><topic>Technological Innovation and Resources</topic><topic>top-down proteomics</topic><topic>Ubiquitin</topic><topic>Ultraviolet Rays</topic><topic>UVPD</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fornelli, Luca</creatorcontrib><creatorcontrib>Srzentić, Kristina</creatorcontrib><creatorcontrib>Toby, Timothy K.</creatorcontrib><creatorcontrib>Doubleday, Peter F.</creatorcontrib><creatorcontrib>Huguet, Romain</creatorcontrib><creatorcontrib>Mullen, Christopher</creatorcontrib><creatorcontrib>Melani, Rafael D.</creatorcontrib><creatorcontrib>dos Santos Seckler, Henrique</creatorcontrib><creatorcontrib>DeHart, Caroline J.</creatorcontrib><creatorcontrib>Weisbrod, Chad R.</creatorcontrib><creatorcontrib>Durbin, Kenneth R.</creatorcontrib><creatorcontrib>Greer, Joseph B.</creatorcontrib><creatorcontrib>Early, Bryan P.</creatorcontrib><creatorcontrib>Fellers, Ryan T.</creatorcontrib><creatorcontrib>Zabrouskov, Vlad</creatorcontrib><creatorcontrib>Thomas, Paul M.</creatorcontrib><creatorcontrib>Compton, Philip D.</creatorcontrib><creatorcontrib>Kelleher, Neil L.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Molecular & cellular proteomics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fornelli, Luca</au><au>Srzentić, Kristina</au><au>Toby, Timothy K.</au><au>Doubleday, Peter F.</au><au>Huguet, Romain</au><au>Mullen, Christopher</au><au>Melani, Rafael D.</au><au>dos Santos Seckler, Henrique</au><au>DeHart, Caroline J.</au><au>Weisbrod, Chad R.</au><au>Durbin, Kenneth R.</au><au>Greer, Joseph B.</au><au>Early, Bryan P.</au><au>Fellers, Ryan T.</au><au>Zabrouskov, Vlad</au><au>Thomas, Paul M.</au><au>Compton, Philip D.</au><au>Kelleher, Neil L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Thorough Performance Evaluation of 213 nm Ultraviolet Photodissociation for Top-down Proteomics</atitle><jtitle>Molecular & cellular proteomics</jtitle><addtitle>Mol Cell Proteomics</addtitle><date>2020-02-01</date><risdate>2020</risdate><volume>19</volume><issue>2</issue><spage>405</spage><epage>420</epage><pages>405-420</pages><issn>1535-9476</issn><eissn>1535-9484</eissn><abstract>We benchmarked ultraviolet photodissociation (UVPD) based on 213 nm photons for the characterization of proteoforms <30 kDa from three different samples (Pseudomonas aeruginosa, mouse hearts and human fibroblasts). Product ion abundance analysis of 213 nm UVPD data sets was used for improving the database search ultimately leading to increased identification rates. 213 nm UVPD outperformed HCD in terms of proteoform characterization (defined by the C-score). Finally, we described UVPD fragmentation propensities and the observation of a 213 nm UVPD-specific product ion.
[Display omitted]
Highlights
•Analysis of product ions produced by 213 nm UVPD is used to refine database search.•A product ion at the N-terminus of Pro, y-2, is observed in 213 nm UVPD spectra.•213 nm UVPD provides more complete proteoform characterization than HCD.•HCD and 213 nm UVPD are complementary fragmentation methods for proteoforms <30 kDa.
Top-down proteomics studies intact proteoform mixtures and offers important advantages over more common bottom-up proteomics technologies, as it avoids the protein inference problem. However, achieving complete molecular characterization of investigated proteoforms using existing technologies remains a fundamental challenge for top-down proteomics. Here, we benchmark the performance of ultraviolet photodissociation (UVPD) using 213 nm photons generated by a solid-state laser applied to the study of intact proteoforms from three organisms. Notably, the described UVPD setup applies multiple laser pulses to induce ion dissociation, and this feature can be used to optimize the fragmentation outcome based on the molecular weight of the analyzed biomolecule. When applied to complex proteoform mixtures in high-throughput top-down proteomics, 213 nm UVPD demonstrated a high degree of complementarity with the most employed fragmentation method in proteomics studies, higher-energy collisional dissociation (HCD). UVPD at 213 nm offered higher average proteoform sequence coverage and degree of proteoform characterization (including localization of post-translational modifications) than HCD. However, previous studies have shown limitations in applying database search strategies developed for HCD fragmentation to UVPD spectra which contains up to nine fragment ion types. We therefore performed an analysis of the different UVPD product ion type frequencies. From these data, we developed an ad hoc fragment matching strategy and determined the influence of each possible ion type on search outcomes. By paring down the number of ion types considered in high-throughput UVPD searches from all types down to the four most abundant, we were ultimately able to achieve deeper proteome characterization with UVPD. Lastly, our detailed product ion analysis also revealed UVPD cleavage propensities and determined the presence of a product ion produced specifically by 213 nm photons. All together, these observations could be used to better elucidate UVPD dissociation mechanisms and improve the utility of the technique for proteomic applications.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>31888965</pmid><doi>10.1074/mcp.TIR119.001638</doi><tpages>16</tpages><orcidid>https://orcid.org/0000-0001-6334-1046</orcidid><orcidid>https://orcid.org/0000-0002-8815-3372</orcidid><orcidid>https://orcid.org/0000-0003-2887-4765</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | Molecular & cellular proteomics, 2020-02, Vol.19 (2), p.405-420 |
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| subjects | Animals Carbonic Anhydrases Cells, Cultured Chromatography, Liquid FDR Fibroblasts Fourier transform MS Fungal Proteins Humans mass spectrometry Mice Myocytes, Cardiac Myoglobin Photons post-translational modifications product ion protein identification proteoform Proteomics - methods Pseudomonas aeruginosa Tandem Mass Spectrometry Technological Innovation and Resources top-down proteomics Ubiquitin Ultraviolet Rays UVPD |
| title | Thorough Performance Evaluation of 213 nm Ultraviolet Photodissociation for Top-down Proteomics |
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