Protonation thermochemistry of alpha-aminoacids bearing a basic residue
The proton affinity, PA, and protonation entropy, Delta(p)S degree, of glycine (Gly), 1, aspartic acid (Asp), 2, asparagine (Asn), 3, histidine (His), 4, lysine (Lys), 5, glutamic acid (Glu), 6, and glutamine (Gln), 7, have been reinvestigated by the extended kinetic method, using the "isotherm...
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| Veröffentlicht in: | European journal of mass spectrometry (Chichester, England) England), 2004, Vol.10 (6), p.977-992 |
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| container_title | European journal of mass spectrometry (Chichester, England) |
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| creator | Bouchoux, Guy Buisson, David-Alexandre Colas, Cyril Sablier, Michel |
| description | The proton affinity, PA, and protonation entropy, Delta(p)S degree, of glycine (Gly), 1, aspartic acid (Asp), 2, asparagine (Asn), 3, histidine (His), 4, lysine (Lys), 5, glutamic acid (Glu), 6, and glutamine (Gln), 7, have been reinvestigated by the extended kinetic method, using the "isothermal point" method and the orthogonal distance regression, ODR, technique. The proton affinity values of a-aminoacids bearing a basic residue (PA = 926.8; 965.2; 996.0; 993.9; 981.8 and 988.1 kJ.mol(-1) for 2-7, respectively) show significant deviation from the tabulated values. As expected from the effect of a strong intramolecular hydrogen bond in the protonated forms of these peculiar aminoacids, negative protonation entropies are detected (Delta(p)S degree = 36; 43; 37; 29; 95 and 55 J mol(-1) K(-1) for for 27 respectively). |
| doi_str_mv | 10.1255/ejms.687 |
| format | Article |
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The proton affinity values of a-aminoacids bearing a basic residue (PA = 926.8; 965.2; 996.0; 993.9; 981.8 and 988.1 kJ.mol(-1) for 2-7, respectively) show significant deviation from the tabulated values. As expected from the effect of a strong intramolecular hydrogen bond in the protonated forms of these peculiar aminoacids, negative protonation entropies are detected (Delta(p)S degree = 36; 43; 37; 29; 95 and 55 J mol(-1) K(-1) for for 27 respectively).</description><identifier>ISSN: 1469-0667</identifier><identifier>DOI: 10.1255/ejms.687</identifier><identifier>PMID: 15775057</identifier><language>eng</language><publisher>England: IM Publications</publisher><subject>Amino Acids - chemistry ; Chemical Sciences ; Entropy ; Glycine - chemistry ; or physical chemistry ; Protons ; Spectrometry, Mass, Electrospray Ionization - methods ; Theoretical and</subject><ispartof>European journal of mass spectrometry (Chichester, England), 2004, Vol.10 (6), p.977-992</ispartof><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><orcidid>0000-0003-1651-6813 ; 0000-0001-6508-8566</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,4009,27902,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15775057$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://polytechnique.hal.science/hal-00916219$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Bouchoux, Guy</creatorcontrib><creatorcontrib>Buisson, David-Alexandre</creatorcontrib><creatorcontrib>Colas, Cyril</creatorcontrib><creatorcontrib>Sablier, Michel</creatorcontrib><title>Protonation thermochemistry of alpha-aminoacids bearing a basic residue</title><title>European journal of mass spectrometry (Chichester, England)</title><addtitle>Eur J Mass Spectrom (Chichester)</addtitle><description>The proton affinity, PA, and protonation entropy, Delta(p)S degree, of glycine (Gly), 1, aspartic acid (Asp), 2, asparagine (Asn), 3, histidine (His), 4, lysine (Lys), 5, glutamic acid (Glu), 6, and glutamine (Gln), 7, have been reinvestigated by the extended kinetic method, using the "isothermal point" method and the orthogonal distance regression, ODR, technique. The proton affinity values of a-aminoacids bearing a basic residue (PA = 926.8; 965.2; 996.0; 993.9; 981.8 and 988.1 kJ.mol(-1) for 2-7, respectively) show significant deviation from the tabulated values. As expected from the effect of a strong intramolecular hydrogen bond in the protonated forms of these peculiar aminoacids, negative protonation entropies are detected (Delta(p)S degree = 36; 43; 37; 29; 95 and 55 J mol(-1) K(-1) for for 27 respectively).</description><subject>Amino Acids - chemistry</subject><subject>Chemical Sciences</subject><subject>Entropy</subject><subject>Glycine - chemistry</subject><subject>or physical chemistry</subject><subject>Protons</subject><subject>Spectrometry, Mass, Electrospray Ionization - methods</subject><subject>Theoretical and</subject><issn>1469-0667</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kEFLwzAYhnNQ3JyCv0ByEjx0Jk2TNMcxdBMGeti9fG2-2Yy2mUkr7N_bsenphZeHB96XkAfO5jyV8gX3bZyrXF-RKc-USZhSekJuY9wzJnNlzA2ZcKm1ZFJPyeoz-N530Dvf0b7G0PqqxtbFPhyp31FoDjUk0LrOQ-VspCVCcN0XBVpCdBUNGJ0d8I5c76CJeH_JGdm-vW6X62TzsXpfLjZJnec6QWYyVY4KgZWBnS0rYbTOrWEAiqPmRjArNbe5QlUKYZVEkY0zMonSZpmYkeeztoamOATXQjgWHlyxXmyKU8eY4Srl5oeP7NOZPQT_PWDsi3FWhU0DHfohFkqnmnGTjuDjBRzKFu2_9-8l8QvCWWYj</recordid><startdate>2004</startdate><enddate>2004</enddate><creator>Bouchoux, Guy</creator><creator>Buisson, David-Alexandre</creator><creator>Colas, Cyril</creator><creator>Sablier, Michel</creator><general>IM Publications</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0003-1651-6813</orcidid><orcidid>https://orcid.org/0000-0001-6508-8566</orcidid></search><sort><creationdate>2004</creationdate><title>Protonation thermochemistry of alpha-aminoacids bearing a basic residue</title><author>Bouchoux, Guy ; Buisson, David-Alexandre ; Colas, Cyril ; Sablier, Michel</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-h887-e0946bbea3ec9afdbc39778d90aa61e71930d571d86e6b33d65e3414645e5d443</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Amino Acids - chemistry</topic><topic>Chemical Sciences</topic><topic>Entropy</topic><topic>Glycine - chemistry</topic><topic>or physical chemistry</topic><topic>Protons</topic><topic>Spectrometry, Mass, Electrospray Ionization - methods</topic><topic>Theoretical and</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bouchoux, Guy</creatorcontrib><creatorcontrib>Buisson, David-Alexandre</creatorcontrib><creatorcontrib>Colas, Cyril</creatorcontrib><creatorcontrib>Sablier, Michel</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>European journal of mass spectrometry (Chichester, England)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bouchoux, Guy</au><au>Buisson, David-Alexandre</au><au>Colas, Cyril</au><au>Sablier, Michel</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Protonation thermochemistry of alpha-aminoacids bearing a basic residue</atitle><jtitle>European journal of mass spectrometry (Chichester, England)</jtitle><addtitle>Eur J Mass Spectrom (Chichester)</addtitle><date>2004</date><risdate>2004</risdate><volume>10</volume><issue>6</issue><spage>977</spage><epage>992</epage><pages>977-992</pages><issn>1469-0667</issn><abstract>The proton affinity, PA, and protonation entropy, Delta(p)S degree, of glycine (Gly), 1, aspartic acid (Asp), 2, asparagine (Asn), 3, histidine (His), 4, lysine (Lys), 5, glutamic acid (Glu), 6, and glutamine (Gln), 7, have been reinvestigated by the extended kinetic method, using the "isothermal point" method and the orthogonal distance regression, ODR, technique. The proton affinity values of a-aminoacids bearing a basic residue (PA = 926.8; 965.2; 996.0; 993.9; 981.8 and 988.1 kJ.mol(-1) for 2-7, respectively) show significant deviation from the tabulated values. As expected from the effect of a strong intramolecular hydrogen bond in the protonated forms of these peculiar aminoacids, negative protonation entropies are detected (Delta(p)S degree = 36; 43; 37; 29; 95 and 55 J mol(-1) K(-1) for for 27 respectively).</abstract><cop>England</cop><pub>IM Publications</pub><pmid>15775057</pmid><doi>10.1255/ejms.687</doi><tpages>16</tpages><orcidid>https://orcid.org/0000-0003-1651-6813</orcidid><orcidid>https://orcid.org/0000-0001-6508-8566</orcidid></addata></record> |
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| subjects | Amino Acids - chemistry Chemical Sciences Entropy Glycine - chemistry or physical chemistry Protons Spectrometry, Mass, Electrospray Ionization - methods Theoretical and |
| title | Protonation thermochemistry of alpha-aminoacids bearing a basic residue |
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