Electron capture dissociation of gaseous multiply charged ions by fourier-transform ion cyclotron resonance
Fourier-transform ion cyclotron resonance instrumentation is uniquely applicable to an unusual new ion chemistry, electron capture dissociation (ECD). This causes nonergodic dissociation of far larger molecules (42 kDa) than previously observed (10 kDa) ions give far more extensive ECD if they are f...
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| Veröffentlicht in: | Journal of the American Society for Mass Spectrometry 2001-03, Vol.12 (3), p.245-249 |
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| container_title | Journal of the American Society for Mass Spectrometry |
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| creator | McLafferty, Fred W Horn, David M Breuker, Kathrin Ge, Ying Lewis, Mark A Cerda, Blas Zubarev, Roman A Carpenter, Barry K |
| description | Fourier-transform ion cyclotron resonance instrumentation is uniquely applicable to an unusual new ion chemistry, electron capture dissociation (ECD). This causes nonergodic dissociation of far larger molecules (42 kDa) than previously observed (10 kDa) ions give far more extensive ECD if they are first thermally activated. This high specificity for covalent bond cleavage also makes ECD promising for studying the secondary and tertiary structure of gaseous protein ions caused by noncovalent bonding. |
| doi_str_mv | 10.1016/S1044-0305(00)00223-3 |
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This causes nonergodic dissociation of far larger molecules (42 kDa) than previously observed (<1 kDa), with the resulting unimolecular ion chemistry also unique because it involves radical site reactions for similarly larger ions. ECD is highly complementary to the well known energetic methods for multiply charged ion dissociation, providing much more extensive protein sequence information, including the direct identification of N- versus C-terminal fragment ions. Because ECD only excites the molecule near the cleavage site, accompanying rearrangements are minimized. Counterintuitively, cleavage of backbone covalent bonds of protein ions is favored over that of noncovalent bonds; larger (>10 kDa) ions give far more extensive ECD if they are first thermally activated. 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This high specificity for covalent bond cleavage also makes ECD promising for studying the secondary and tertiary structure of gaseous protein ions caused by noncovalent bonding.</description><subject>Beta decay</subject><subject>Chemical bonds</subject><subject>Cleavage</subject><subject>Covalent bonds</subject><subject>Cyclotron resonance</subject><subject>Cyclotrons</subject><subject>Electron capture</subject><subject>Fourier Analysis</subject><subject>Fourier transforms</subject><subject>Ions</subject><subject>Mass spectrometry</subject><subject>Mass Spectrometry - instrumentation</subject><subject>Mass Spectrometry - methods</subject><subject>Protein Conformation</subject><subject>Proteins</subject><subject>Proteins - chemistry</subject><subject>Proteome - analysis</subject><subject>Sequence Analysis, Protein</subject><issn>1044-0305</issn><issn>1879-1123</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqFkU2L1TAUhosozjj6E5SAILqonnwnq0GG8QMGXKjrkKanY8a2uSatcP-96b1XBBe6SULOk_fkvG_TPKXwmgJVbz5TEKIFDvIlwCsAxnjL7zXn1GjbUsr4_Xr-jZw1j0q5A6AarH7YnNW6odLa8-b79YhhyWkmwe-WNSPpYykpRL_EepkGcusLprWQaR2XuBv3JHzz-RZ7UuuFdHsypDVHzO2S_VyGlKetQsI-jOkgnLGk2c8BHzcPBj8WfHLaL5qv766_XH1obz69_3j19qYNwvCllSFIZjomjNRMM2Zk6LyCTqDuDVIRFDW9ZQGV8Vb5jimUwhrNey4HVdeL5sVRd5fTjxXL4qZYAo6jn7dJnNZAwWhawed_gXd1lrn-zTGlJOWy-vgvilrJhAAubKXkkQo5lZJxcLscJ5_3joLbEnOHxNwWhwNwh8Tcpv7spL52E_Z_Xp0iqsDlEcBq2c9qtCshYrWzj7lG5_oU_9PiF-5YpU4</recordid><startdate>20010301</startdate><enddate>20010301</enddate><creator>McLafferty, Fred W</creator><creator>Horn, David M</creator><creator>Breuker, Kathrin</creator><creator>Ge, Ying</creator><creator>Lewis, Mark A</creator><creator>Cerda, Blas</creator><creator>Zubarev, Roman A</creator><creator>Carpenter, Barry K</creator><general>Elsevier Inc</general><general>Springer Nature B.V</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>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FE</scope><scope>8FG</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>MBDVC</scope><scope>P5Z</scope><scope>P62</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope></search><sort><creationdate>20010301</creationdate><title>Electron capture dissociation of gaseous multiply charged ions by fourier-transform ion cyclotron resonance</title><author>McLafferty, Fred W ; 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This causes nonergodic dissociation of far larger molecules (42 kDa) than previously observed (<1 kDa), with the resulting unimolecular ion chemistry also unique because it involves radical site reactions for similarly larger ions. ECD is highly complementary to the well known energetic methods for multiply charged ion dissociation, providing much more extensive protein sequence information, including the direct identification of N- versus C-terminal fragment ions. Because ECD only excites the molecule near the cleavage site, accompanying rearrangements are minimized. Counterintuitively, cleavage of backbone covalent bonds of protein ions is favored over that of noncovalent bonds; larger (>10 kDa) ions give far more extensive ECD if they are first thermally activated. 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| subjects | Beta decay Chemical bonds Cleavage Covalent bonds Cyclotron resonance Cyclotrons Electron capture Fourier Analysis Fourier transforms Ions Mass spectrometry Mass Spectrometry - instrumentation Mass Spectrometry - methods Protein Conformation Proteins Proteins - chemistry Proteome - analysis Sequence Analysis, Protein |
| title | Electron capture dissociation of gaseous multiply charged ions by fourier-transform ion cyclotron resonance |
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