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Effects of solvent on the maximum charge state and charge state distribution of protein ions produced by electrospray ionization
The effects of solvent composition on both the maximum charge states and charge state distributions of analyte ions formed by electrospray ionization were investigated using a quadrupole mass spectrometer. The charge state distributions of cytochrome c and myoglobin, formed from 47%/50%/3% water/sol...
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| Published in: | Journal of the American Society for Mass Spectrometry 2000-11, Vol.11 (11), p.976-985 |
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| cites | cdi_FETCH-LOGICAL-c585t-e0e944c0249bf84f579a55fe599f924d50962120552f9118264d30b60e0941b43 |
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| container_issue | 11 |
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| container_title | Journal of the American Society for Mass Spectrometry |
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| creator | Iavarone, Anthony T Jurchen, John C Williams, Evan R |
| description | The effects of solvent composition on both the maximum charge states and charge state distributions of analyte ions formed by electrospray ionization were investigated using a quadrupole mass spectrometer. The charge state distributions of cytochrome
c and myoglobin, formed from 47%/50%/3% water/solvent/acetic acid solutions, shift to lower charge (higher
m/z) when the 50% solvent fraction is changed from water to methanol, to acetonitrile, to isopropanol. This is also the order of increasing gas-phase basicities of these solvents, although other physical properties of these solvents may also play a role. The effect is relatively small for these solvents, possibly due to their limited concentration inside the electrospray interface. In contrast, the addition of even small amounts of diethylamine ( |
| doi_str_mv | 10.1016/S1044-0305(00)00169-0 |
| format | article |
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c and myoglobin, formed from 47%/50%/3% water/solvent/acetic acid solutions, shift to lower charge (higher
m/z) when the 50% solvent fraction is changed from water to methanol, to acetonitrile, to isopropanol. This is also the order of increasing gas-phase basicities of these solvents, although other physical properties of these solvents may also play a role. The effect is relatively small for these solvents, possibly due to their limited concentration inside the electrospray interface. In contrast, the addition of even small amounts of diethylamine (<0.4%) results in dramatic shifts to lower charge, presumably due to preferential proton transfer from the higher charge state ions to diethylamine. These results clearly show that the maximum charge states and charge state distributions of ions formed by electrospray ionization are influenced by solvents that are more volatile than water. Addition of even small amounts of two solvents that are less volatile than water, ethylene glycol and 2-methoxyethanol, also results in preferential deprotonation of higher charge state ions of small peptides, but these solvents actually produce an
enhancement in the higher charge state ions for both cytochrome
c and myoglobin. For instruments that have capabilities that improve with lower
m/z, this effect could be taken advantage of to improve the performance of an analysis.</description><identifier>ISSN: 1044-0305</identifier><identifier>EISSN: 1879-1123</identifier><identifier>DOI: 10.1016/S1044-0305(00)00169-0</identifier><identifier>PMID: 11073261</identifier><language>eng</language><publisher>New York, NY: Elsevier Inc</publisher><subject>Acetic acid ; Acetonitrile ; Algorithms ; Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; Charge distribution ; Charge transfer ; Composition effects ; Cytochrome ; Cytochrome c Group - chemistry ; Diethylamines - chemistry ; Electrospraying ; Ethylene glycol ; Fundamental and applied biological sciences. Psychology ; Hemoproteins ; Hydrogen-Ion Concentration ; Ionization ; Ions ; Mass spectrometry ; Metalloproteins ; Methyl cellosolve ; Myoglobin - chemistry ; Myoglobins ; Peptides ; Peptides - chemistry ; Performance enhancement ; Physical properties ; Proteins ; Proteins - chemistry ; Quadrupoles ; Solvents ; Spectrometry, Mass, Electrospray Ionization - methods ; Volatilization</subject><ispartof>Journal of the American Society for Mass Spectrometry, 2000-11, Vol.11 (11), p.976-985</ispartof><rights>2000 American Society for Mass Spectrometry</rights><rights>2001 INIST-CNRS</rights><rights>American Society for Mass Spectrometry 2000</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c585t-e0e944c0249bf84f579a55fe599f924d50962120552f9118264d30b60e0941b43</citedby><cites>FETCH-LOGICAL-c585t-e0e944c0249bf84f579a55fe599f924d50962120552f9118264d30b60e0941b43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=797496$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11073261$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Iavarone, Anthony T</creatorcontrib><creatorcontrib>Jurchen, John C</creatorcontrib><creatorcontrib>Williams, Evan R</creatorcontrib><title>Effects of solvent on the maximum charge state and charge state distribution of protein ions produced by electrospray ionization</title><title>Journal of the American Society for Mass Spectrometry</title><addtitle>J Am Soc Mass Spectrom</addtitle><description>The effects of solvent composition on both the maximum charge states and charge state distributions of analyte ions formed by electrospray ionization were investigated using a quadrupole mass spectrometer. The charge state distributions of cytochrome
c and myoglobin, formed from 47%/50%/3% water/solvent/acetic acid solutions, shift to lower charge (higher
m/z) when the 50% solvent fraction is changed from water to methanol, to acetonitrile, to isopropanol. This is also the order of increasing gas-phase basicities of these solvents, although other physical properties of these solvents may also play a role. The effect is relatively small for these solvents, possibly due to their limited concentration inside the electrospray interface. In contrast, the addition of even small amounts of diethylamine (<0.4%) results in dramatic shifts to lower charge, presumably due to preferential proton transfer from the higher charge state ions to diethylamine. These results clearly show that the maximum charge states and charge state distributions of ions formed by electrospray ionization are influenced by solvents that are more volatile than water. Addition of even small amounts of two solvents that are less volatile than water, ethylene glycol and 2-methoxyethanol, also results in preferential deprotonation of higher charge state ions of small peptides, but these solvents actually produce an
enhancement in the higher charge state ions for both cytochrome
c and myoglobin. For instruments that have capabilities that improve with lower
m/z, this effect could be taken advantage of to improve the performance of an analysis.</description><subject>Acetic acid</subject><subject>Acetonitrile</subject><subject>Algorithms</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Charge distribution</subject><subject>Charge transfer</subject><subject>Composition effects</subject><subject>Cytochrome</subject><subject>Cytochrome c Group - chemistry</subject><subject>Diethylamines - chemistry</subject><subject>Electrospraying</subject><subject>Ethylene glycol</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hemoproteins</subject><subject>Hydrogen-Ion Concentration</subject><subject>Ionization</subject><subject>Ions</subject><subject>Mass spectrometry</subject><subject>Metalloproteins</subject><subject>Methyl cellosolve</subject><subject>Myoglobin - chemistry</subject><subject>Myoglobins</subject><subject>Peptides</subject><subject>Peptides - chemistry</subject><subject>Performance enhancement</subject><subject>Physical properties</subject><subject>Proteins</subject><subject>Proteins - chemistry</subject><subject>Quadrupoles</subject><subject>Solvents</subject><subject>Spectrometry, Mass, Electrospray Ionization - methods</subject><subject>Volatilization</subject><issn>1044-0305</issn><issn>1879-1123</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><recordid>eNqFkU1v1DAQhiMEomXhJ4AsISE4BMaOHceXIlSVD6kSB-BsOc646yqJFztZsT31p-N0l9Jy4WTPzDOfb1E8p_CWAq3ffaPAeQkViNcAbyC7VAkPimPaSFVSyqqH-f8HOSqepHSZIQlKPi6OKAVZsZoeF9dnzqGdEgmOpNBvcZxIGMm0RjKYX36YB2LXJl4gSZOZkJixu-_ofJqib-fJ57RcZBPDhH4k2UyL0c0WO9LuCPa5TwxpE81uifors-Q8LR450yd8dnhXxY-PZ99PP5fnXz99Of1wXlrRiKlEQMW5BcZV6xruhFRGCIdCKacY7wSomlEGQjCnKG1YzbsK2hoQFKctr1bFyb7uZm4H7GxeNJpeb6IfTNzpYLy-Hxn9Wl-EraaccqmWAq8OBWL4OWOa9OCTxb43I4Y5ackqJRvZZPDlP-BlmOOYl9NUCcYrWUuVKbGnbL5JiuhuR6GgF4X1jcJ6kU8D6BuFs7UqXtzd42_WQdI77U2ypnfRjNanW04qyVWdqfd7CvPNtx6jTtbjmLXyMeuku-D_M8hvkIvDvQ</recordid><startdate>20001101</startdate><enddate>20001101</enddate><creator>Iavarone, Anthony T</creator><creator>Jurchen, John C</creator><creator>Williams, Evan R</creator><general>Elsevier Inc</general><general>Elsevier Science</general><general>Springer Nature B.V</general><scope>6I.</scope><scope>AAFTH</scope><scope>IQODW</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>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20001101</creationdate><title>Effects of solvent on the maximum charge state and charge state distribution of protein ions produced by electrospray ionization</title><author>Iavarone, Anthony T ; Jurchen, John C ; Williams, Evan R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c585t-e0e944c0249bf84f579a55fe599f924d50962120552f9118264d30b60e0941b43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Acetic acid</topic><topic>Acetonitrile</topic><topic>Algorithms</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Biological and medical sciences</topic><topic>Charge distribution</topic><topic>Charge transfer</topic><topic>Composition effects</topic><topic>Cytochrome</topic><topic>Cytochrome c Group - chemistry</topic><topic>Diethylamines - chemistry</topic><topic>Electrospraying</topic><topic>Ethylene glycol</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hemoproteins</topic><topic>Hydrogen-Ion Concentration</topic><topic>Ionization</topic><topic>Ions</topic><topic>Mass spectrometry</topic><topic>Metalloproteins</topic><topic>Methyl cellosolve</topic><topic>Myoglobin - chemistry</topic><topic>Myoglobins</topic><topic>Peptides</topic><topic>Peptides - chemistry</topic><topic>Performance enhancement</topic><topic>Physical properties</topic><topic>Proteins</topic><topic>Proteins - chemistry</topic><topic>Quadrupoles</topic><topic>Solvents</topic><topic>Spectrometry, Mass, Electrospray Ionization - methods</topic><topic>Volatilization</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Iavarone, Anthony T</creatorcontrib><creatorcontrib>Jurchen, John C</creatorcontrib><creatorcontrib>Williams, Evan R</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Research Library (Corporate)</collection><collection>Advanced Technologies & Aerospace Database</collection><collection>ProQuest Advanced Technologies & Aerospace Collection</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of the American Society for Mass Spectrometry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Iavarone, Anthony T</au><au>Jurchen, John C</au><au>Williams, Evan R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Effects of solvent on the maximum charge state and charge state distribution of protein ions produced by electrospray ionization</atitle><jtitle>Journal of the American Society for Mass Spectrometry</jtitle><addtitle>J Am Soc Mass Spectrom</addtitle><date>2000-11-01</date><risdate>2000</risdate><volume>11</volume><issue>11</issue><spage>976</spage><epage>985</epage><pages>976-985</pages><issn>1044-0305</issn><eissn>1879-1123</eissn><abstract>The effects of solvent composition on both the maximum charge states and charge state distributions of analyte ions formed by electrospray ionization were investigated using a quadrupole mass spectrometer. The charge state distributions of cytochrome
c and myoglobin, formed from 47%/50%/3% water/solvent/acetic acid solutions, shift to lower charge (higher
m/z) when the 50% solvent fraction is changed from water to methanol, to acetonitrile, to isopropanol. This is also the order of increasing gas-phase basicities of these solvents, although other physical properties of these solvents may also play a role. The effect is relatively small for these solvents, possibly due to their limited concentration inside the electrospray interface. In contrast, the addition of even small amounts of diethylamine (<0.4%) results in dramatic shifts to lower charge, presumably due to preferential proton transfer from the higher charge state ions to diethylamine. These results clearly show that the maximum charge states and charge state distributions of ions formed by electrospray ionization are influenced by solvents that are more volatile than water. Addition of even small amounts of two solvents that are less volatile than water, ethylene glycol and 2-methoxyethanol, also results in preferential deprotonation of higher charge state ions of small peptides, but these solvents actually produce an
enhancement in the higher charge state ions for both cytochrome
c and myoglobin. For instruments that have capabilities that improve with lower
m/z, this effect could be taken advantage of to improve the performance of an analysis.</abstract><cop>New York, NY</cop><pub>Elsevier Inc</pub><pmid>11073261</pmid><doi>10.1016/S1044-0305(00)00169-0</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Journal of the American Society for Mass Spectrometry, 2000-11, Vol.11 (11), p.976-985 |
| issn | 1044-0305 1879-1123 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1414794 |
| source | American Chemical Society:Jisc Collections:American Chemical Society Read & Publish Agreement 2022-2024 (Reading list) |
| subjects | Acetic acid Acetonitrile Algorithms Analytical, structural and metabolic biochemistry Biological and medical sciences Charge distribution Charge transfer Composition effects Cytochrome Cytochrome c Group - chemistry Diethylamines - chemistry Electrospraying Ethylene glycol Fundamental and applied biological sciences. Psychology Hemoproteins Hydrogen-Ion Concentration Ionization Ions Mass spectrometry Metalloproteins Methyl cellosolve Myoglobin - chemistry Myoglobins Peptides Peptides - chemistry Performance enhancement Physical properties Proteins Proteins - chemistry Quadrupoles Solvents Spectrometry, Mass, Electrospray Ionization - methods Volatilization |
| title | Effects of solvent on the maximum charge state and charge state distribution of protein ions produced by electrospray ionization |
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