Electron Capture Dissociation as Structural Probe for Noncovalent Gas-Phase Protein Assemblies
Electron capture dissociation (ECD) of proteins in Fourier transform ion cyclotron resonance mass spectrometry usually leads to charge reduction and backbone-bond cleavage, thereby mostly retaining labile, intramolecular noncovalent interactions. In this report, we evaluate ECD of the 84-kDa noncova...
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| Veröffentlicht in: | Analytical chemistry (Washington) 2006-10, Vol.78 (20), p.7191-7196 |
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| creator | Geels, Rimco B. J van der Vies, Saskia M Heck, Albert J. R Heeren, Ron M. A |
| description | Electron capture dissociation (ECD) of proteins in Fourier transform ion cyclotron resonance mass spectrometry usually leads to charge reduction and backbone-bond cleavage, thereby mostly retaining labile, intramolecular noncovalent interactions. In this report, we evaluate ECD of the 84-kDa noncovalent heptameric gp31 complex and compare this with sustained off-resonance irradiation collisionally activated dissociation (SORI-CAD) of the same protein. Unexpectedly, the 21+ charge state of the gp31 oligomer exhibits a main ECD pathway resulting in a hexamer and monomer, disrupting labile, intermolecular noncovalent bonds and leaving the backbone intact. Unexpectedly, the charge separation over the two products is highly proportional to molecular weight. This indicates that a major charge redistribution over the subunits of the complex does not take place during ECD, in contrast to the behavior observed when using SORI-CAD. We speculate that the ejected monomer retains more of its original structure in ECD, when compared to SORI-CAD. ECD of lower charge states of gp31 does not lead to dissociation of noncovalent bonds. We hypothesize that the initial gas-phase structure of the 21+ charge state is significantly different from the lower charge states. These structural differences result in the different reaction pathways when using ECD. |
| doi_str_mv | 10.1021/ac060960p |
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J ; van der Vies, Saskia M ; Heck, Albert J. R ; Heeren, Ron M. A</creator><creatorcontrib>Geels, Rimco B. J ; van der Vies, Saskia M ; Heck, Albert J. R ; Heeren, Ron M. A</creatorcontrib><description>Electron capture dissociation (ECD) of proteins in Fourier transform ion cyclotron resonance mass spectrometry usually leads to charge reduction and backbone-bond cleavage, thereby mostly retaining labile, intramolecular noncovalent interactions. In this report, we evaluate ECD of the 84-kDa noncovalent heptameric gp31 complex and compare this with sustained off-resonance irradiation collisionally activated dissociation (SORI-CAD) of the same protein. Unexpectedly, the 21+ charge state of the gp31 oligomer exhibits a main ECD pathway resulting in a hexamer and monomer, disrupting labile, intermolecular noncovalent bonds and leaving the backbone intact. Unexpectedly, the charge separation over the two products is highly proportional to molecular weight. This indicates that a major charge redistribution over the subunits of the complex does not take place during ECD, in contrast to the behavior observed when using SORI-CAD. We speculate that the ejected monomer retains more of its original structure in ECD, when compared to SORI-CAD. ECD of lower charge states of gp31 does not lead to dissociation of noncovalent bonds. We hypothesize that the initial gas-phase structure of the 21+ charge state is significantly different from the lower charge states. 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J</creatorcontrib><creatorcontrib>van der Vies, Saskia M</creatorcontrib><creatorcontrib>Heck, Albert J. R</creatorcontrib><creatorcontrib>Heeren, Ron M. A</creatorcontrib><title>Electron Capture Dissociation as Structural Probe for Noncovalent Gas-Phase Protein Assemblies</title><title>Analytical chemistry (Washington)</title><addtitle>Anal. Chem</addtitle><description>Electron capture dissociation (ECD) of proteins in Fourier transform ion cyclotron resonance mass spectrometry usually leads to charge reduction and backbone-bond cleavage, thereby mostly retaining labile, intramolecular noncovalent interactions. In this report, we evaluate ECD of the 84-kDa noncovalent heptameric gp31 complex and compare this with sustained off-resonance irradiation collisionally activated dissociation (SORI-CAD) of the same protein. Unexpectedly, the 21+ charge state of the gp31 oligomer exhibits a main ECD pathway resulting in a hexamer and monomer, disrupting labile, intermolecular noncovalent bonds and leaving the backbone intact. Unexpectedly, the charge separation over the two products is highly proportional to molecular weight. This indicates that a major charge redistribution over the subunits of the complex does not take place during ECD, in contrast to the behavior observed when using SORI-CAD. We speculate that the ejected monomer retains more of its original structure in ECD, when compared to SORI-CAD. ECD of lower charge states of gp31 does not lead to dissociation of noncovalent bonds. We hypothesize that the initial gas-phase structure of the 21+ charge state is significantly different from the lower charge states. These structural differences result in the different reaction pathways when using ECD.</description><subject>Analytical chemistry</subject><subject>Chaperonins - chemistry</subject><subject>Chaperonins - metabolism</subject><subject>Chemistry</subject><subject>Comparative studies</subject><subject>Dimerization</subject><subject>Electrons</subject><subject>Exact sciences and technology</subject><subject>Glycoproteins - chemistry</subject><subject>Glycoproteins - metabolism</subject><subject>Hypotheses</subject><subject>Mass Spectrometry</subject><subject>Protein Binding</subject><subject>Proteins</subject><subject>Spectrometric and optical methods</subject><subject>Spectroscopy, Fourier Transform Infrared</subject><issn>0003-2700</issn><issn>1520-6882</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpl0N9rFDEQB_Agij2rD_4DsggKfdg6yf5I8liutQqtHtxp3wyTdBa37m2umV1p__tuuaMH-hTIfPgy8xXirYRjCUp-wgA12Bo2z8RMVgry2hj1XMwAoMiVBjgQr5hvAKQEWb8UB1JDoa2Cmfh11lEYUuyzOW6GMVF22jLH0OLQTp_I2XJIY5gm2GWLFD1lTUzZt9iH-Bc76ofsHDlf_Eamx_lAbZ-dMNPady3xa_GiwY7pze49FD8-n63mX_KL7-df5ycXOZZlMeTWEpkglTKWrklWhcTKW92AV1J63yivDGo1XVnKUHlFppFQ-qpGbTUWWByKj9vcTYq3I_Hg1i0H6jrsKY7samMrbaCc4Pt_4E0cUz_t5pTUxoC0xYSOtiikyJyocZvUrjHdOwnusXH31Phk3-0CR7-m673cVTyBDzuAHLBrEvah5b0zSllQ9eTyrWt5oLunOaY_rtaFrtxqsXQ_T6-W9eWVdKt9LgbeH_H_gg_RKqLP</recordid><startdate>20061015</startdate><enddate>20061015</enddate><creator>Geels, Rimco B. 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J</au><au>van der Vies, Saskia M</au><au>Heck, Albert J. R</au><au>Heeren, Ron M. A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Electron Capture Dissociation as Structural Probe for Noncovalent Gas-Phase Protein Assemblies</atitle><jtitle>Analytical chemistry (Washington)</jtitle><addtitle>Anal. Chem</addtitle><date>2006-10-15</date><risdate>2006</risdate><volume>78</volume><issue>20</issue><spage>7191</spage><epage>7196</epage><pages>7191-7196</pages><issn>0003-2700</issn><eissn>1520-6882</eissn><coden>ANCHAM</coden><abstract>Electron capture dissociation (ECD) of proteins in Fourier transform ion cyclotron resonance mass spectrometry usually leads to charge reduction and backbone-bond cleavage, thereby mostly retaining labile, intramolecular noncovalent interactions. In this report, we evaluate ECD of the 84-kDa noncovalent heptameric gp31 complex and compare this with sustained off-resonance irradiation collisionally activated dissociation (SORI-CAD) of the same protein. Unexpectedly, the 21+ charge state of the gp31 oligomer exhibits a main ECD pathway resulting in a hexamer and monomer, disrupting labile, intermolecular noncovalent bonds and leaving the backbone intact. Unexpectedly, the charge separation over the two products is highly proportional to molecular weight. This indicates that a major charge redistribution over the subunits of the complex does not take place during ECD, in contrast to the behavior observed when using SORI-CAD. We speculate that the ejected monomer retains more of its original structure in ECD, when compared to SORI-CAD. ECD of lower charge states of gp31 does not lead to dissociation of noncovalent bonds. We hypothesize that the initial gas-phase structure of the 21+ charge state is significantly different from the lower charge states. These structural differences result in the different reaction pathways when using ECD.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>17037920</pmid><doi>10.1021/ac060960p</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Analytical chemistry Chaperonins - chemistry Chaperonins - metabolism Chemistry Comparative studies Dimerization Electrons Exact sciences and technology Glycoproteins - chemistry Glycoproteins - metabolism Hypotheses Mass Spectrometry Protein Binding Proteins Spectrometric and optical methods Spectroscopy, Fourier Transform Infrared |
| title | Electron Capture Dissociation as Structural Probe for Noncovalent Gas-Phase Protein Assemblies |
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