A Novel Mechanism of Proton Transfer in Protonated Peptides

The study presents quantum-chemical calculations on proton transfer in protonated N-acetylglycyl-N -methylglycinamide (AGA) as a short oligopeptide model. All calculations employ the B3LYP functional and the 6-31++G** basis set. Two different mechanisms of proton transfer are discussed. The rate-det...

Full description

Saved in:
Bibliographic Details
Published in:Journal of the American Chemical Society 2003-11, Vol.125 (45), p.13678-13679
Main Authors: Kulhánek, Petr, Schlag, Edward W, Koča, Jaroslav
Format: Article
Language:English
Subjects:
Atomic and molecular physics
Bond strengths, dissociation energies
Exact sciences and technology
Glycine - analogs & derivatives
Glycine - chemistry
Molecular properties and interactions with photons
Peptides - chemistry
Physics
Properties of molecules and molecular ions
Protein Conformation
Protons
Thermodynamics
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-a379t-7096cde1c4945692ef3182e1d6b0cf6260e32163a28184e0cdb0369f841d422c3
cites cdi_FETCH-LOGICAL-a379t-7096cde1c4945692ef3182e1d6b0cf6260e32163a28184e0cdb0369f841d422c3
container_end_page 13679
container_issue 45
container_start_page 13678
container_title Journal of the American Chemical Society
container_volume 125
creator Kulhánek, Petr
Schlag, Edward W
Koča, Jaroslav
description The study presents quantum-chemical calculations on proton transfer in protonated N-acetylglycyl-N -methylglycinamide (AGA) as a short oligopeptide model. All calculations employ the B3LYP functional and the 6-31++G** basis set. Two different mechanisms of proton transfer are discussed. The rate-determining step of the first mechanism exhibits an energy barrier of about 17.7 kcal mol-1, and it is represented by an isomerization of the proton around the double bond of the carbonyl group. The second mechanism is based on the large conformational flexibility of AGA, where all carbonyl oxygens cooperate. The rate-determining step of this mechanism exhibits an energy barrier of only 8.3 kcal mol-1.
doi_str_mv 10.1021/ja035800z
format article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_71345481</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>71345481</sourcerecordid><originalsourceid>FETCH-LOGICAL-a379t-7096cde1c4945692ef3182e1d6b0cf6260e32163a28184e0cdb0369f841d422c3</originalsourceid><addsrcrecordid>eNptkE1Lw0AQhhdRbP04-AckFwUP0dnPZPFUivWDqgUreFu2mwmmpkndTUX99UYa7MXTMDMPLy8PIUcUzikwejG3wGUK8L1F-lQyiCVlapv0AYDFSap4j-yFMG9XwVK6S3pUSK0Z8D65HEQP9QeW0T26V1sVYRHVeTTxdVNX0dTbKuToo6LqTrbBLJrgsikyDAdkJ7dlwMNu7pPn0dV0eBOPH69vh4NxbHmimzgBrVyG1AktpNIMc05ThjRTM3C5YgqQM6q4bbulAsFlM-BK56mgmWDM8X1yus5d-vp9haExiyI4LEtbYb0KJqFcSJHSFjxbg87XIXjMzdIXC-u_DAXza8r8mWrZ4y50NVtgtiE7NS1w0gE2OFvmrQtXhA0nmWYpiJaL11wRGvz8-1v_ZlTCE2mmkydzL--4frkGM9rkWhfMvF75qnX3T8EfFS-JAA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>71345481</pqid></control><display><type>article</type><title>A Novel Mechanism of Proton Transfer in Protonated Peptides</title><source>Access via American Chemical Society</source><creator>Kulhánek, Petr ; Schlag, Edward W ; Koča, Jaroslav</creator><creatorcontrib>Kulhánek, Petr ; Schlag, Edward W ; Koča, Jaroslav</creatorcontrib><description>The study presents quantum-chemical calculations on proton transfer in protonated N-acetylglycyl-N -methylglycinamide (AGA) as a short oligopeptide model. All calculations employ the B3LYP functional and the 6-31++G** basis set. Two different mechanisms of proton transfer are discussed. The rate-determining step of the first mechanism exhibits an energy barrier of about 17.7 kcal mol-1, and it is represented by an isomerization of the proton around the double bond of the carbonyl group. The second mechanism is based on the large conformational flexibility of AGA, where all carbonyl oxygens cooperate. The rate-determining step of this mechanism exhibits an energy barrier of only 8.3 kcal mol-1.</description><identifier>ISSN: 0002-7863</identifier><identifier>EISSN: 1520-5126</identifier><identifier>DOI: 10.1021/ja035800z</identifier><identifier>PMID: 14599203</identifier><identifier>CODEN: JACSAT</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Atomic and molecular physics ; Bond strengths, dissociation energies ; Exact sciences and technology ; Glycine - analogs &amp; derivatives ; Glycine - chemistry ; Molecular properties and interactions with photons ; Peptides - chemistry ; Physics ; Properties of molecules and molecular ions ; Protein Conformation ; Protons ; Thermodynamics</subject><ispartof>Journal of the American Chemical Society, 2003-11, Vol.125 (45), p.13678-13679</ispartof><rights>Copyright © 2003 American Chemical Society</rights><rights>2004 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a379t-7096cde1c4945692ef3182e1d6b0cf6260e32163a28184e0cdb0369f841d422c3</citedby><cites>FETCH-LOGICAL-a379t-7096cde1c4945692ef3182e1d6b0cf6260e32163a28184e0cdb0369f841d422c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=15292804$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14599203$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kulhánek, Petr</creatorcontrib><creatorcontrib>Schlag, Edward W</creatorcontrib><creatorcontrib>Koča, Jaroslav</creatorcontrib><title>A Novel Mechanism of Proton Transfer in Protonated Peptides</title><title>Journal of the American Chemical Society</title><addtitle>J. Am. Chem. Soc</addtitle><description>The study presents quantum-chemical calculations on proton transfer in protonated N-acetylglycyl-N -methylglycinamide (AGA) as a short oligopeptide model. All calculations employ the B3LYP functional and the 6-31++G** basis set. Two different mechanisms of proton transfer are discussed. The rate-determining step of the first mechanism exhibits an energy barrier of about 17.7 kcal mol-1, and it is represented by an isomerization of the proton around the double bond of the carbonyl group. The second mechanism is based on the large conformational flexibility of AGA, where all carbonyl oxygens cooperate. The rate-determining step of this mechanism exhibits an energy barrier of only 8.3 kcal mol-1.</description><subject>Atomic and molecular physics</subject><subject>Bond strengths, dissociation energies</subject><subject>Exact sciences and technology</subject><subject>Glycine - analogs &amp; derivatives</subject><subject>Glycine - chemistry</subject><subject>Molecular properties and interactions with photons</subject><subject>Peptides - chemistry</subject><subject>Physics</subject><subject>Properties of molecules and molecular ions</subject><subject>Protein Conformation</subject><subject>Protons</subject><subject>Thermodynamics</subject><issn>0002-7863</issn><issn>1520-5126</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><recordid>eNptkE1Lw0AQhhdRbP04-AckFwUP0dnPZPFUivWDqgUreFu2mwmmpkndTUX99UYa7MXTMDMPLy8PIUcUzikwejG3wGUK8L1F-lQyiCVlapv0AYDFSap4j-yFMG9XwVK6S3pUSK0Z8D65HEQP9QeW0T26V1sVYRHVeTTxdVNX0dTbKuToo6LqTrbBLJrgsikyDAdkJ7dlwMNu7pPn0dV0eBOPH69vh4NxbHmimzgBrVyG1AktpNIMc05ThjRTM3C5YgqQM6q4bbulAsFlM-BK56mgmWDM8X1yus5d-vp9haExiyI4LEtbYb0KJqFcSJHSFjxbg87XIXjMzdIXC-u_DAXza8r8mWrZ4y50NVtgtiE7NS1w0gE2OFvmrQtXhA0nmWYpiJaL11wRGvz8-1v_ZlTCE2mmkydzL--4frkGM9rkWhfMvF75qnX3T8EfFS-JAA</recordid><startdate>20031112</startdate><enddate>20031112</enddate><creator>Kulhánek, Petr</creator><creator>Schlag, Edward W</creator><creator>Koča, Jaroslav</creator><general>American Chemical Society</general><scope>BSCLL</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>7X8</scope></search><sort><creationdate>20031112</creationdate><title>A Novel Mechanism of Proton Transfer in Protonated Peptides</title><author>Kulhánek, Petr ; Schlag, Edward W ; Koča, Jaroslav</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a379t-7096cde1c4945692ef3182e1d6b0cf6260e32163a28184e0cdb0369f841d422c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Atomic and molecular physics</topic><topic>Bond strengths, dissociation energies</topic><topic>Exact sciences and technology</topic><topic>Glycine - analogs &amp; derivatives</topic><topic>Glycine - chemistry</topic><topic>Molecular properties and interactions with photons</topic><topic>Peptides - chemistry</topic><topic>Physics</topic><topic>Properties of molecules and molecular ions</topic><topic>Protein Conformation</topic><topic>Protons</topic><topic>Thermodynamics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kulhánek, Petr</creatorcontrib><creatorcontrib>Schlag, Edward W</creatorcontrib><creatorcontrib>Koča, Jaroslav</creatorcontrib><collection>Istex</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>MEDLINE - Academic</collection><jtitle>Journal of the American Chemical Society</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kulhánek, Petr</au><au>Schlag, Edward W</au><au>Koča, Jaroslav</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Novel Mechanism of Proton Transfer in Protonated Peptides</atitle><jtitle>Journal of the American Chemical Society</jtitle><addtitle>J. Am. Chem. Soc</addtitle><date>2003-11-12</date><risdate>2003</risdate><volume>125</volume><issue>45</issue><spage>13678</spage><epage>13679</epage><pages>13678-13679</pages><issn>0002-7863</issn><eissn>1520-5126</eissn><coden>JACSAT</coden><abstract>The study presents quantum-chemical calculations on proton transfer in protonated N-acetylglycyl-N -methylglycinamide (AGA) as a short oligopeptide model. All calculations employ the B3LYP functional and the 6-31++G** basis set. Two different mechanisms of proton transfer are discussed. The rate-determining step of the first mechanism exhibits an energy barrier of about 17.7 kcal mol-1, and it is represented by an isomerization of the proton around the double bond of the carbonyl group. The second mechanism is based on the large conformational flexibility of AGA, where all carbonyl oxygens cooperate. The rate-determining step of this mechanism exhibits an energy barrier of only 8.3 kcal mol-1.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>14599203</pmid><doi>10.1021/ja035800z</doi><tpages>2</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0002-7863
ispartof Journal of the American Chemical Society, 2003-11, Vol.125 (45), p.13678-13679
issn 0002-7863
1520-5126
language eng
recordid cdi_proquest_miscellaneous_71345481
source Access via American Chemical Society
subjects Atomic and molecular physics
Bond strengths, dissociation energies
Exact sciences and technology
Glycine - analogs & derivatives
Glycine - chemistry
Molecular properties and interactions with photons
Peptides - chemistry
Physics
Properties of molecules and molecular ions
Protein Conformation
Protons
Thermodynamics
title A Novel Mechanism of Proton Transfer in Protonated Peptides
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-24T22%3A30%3A03IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=A%20Novel%20Mechanism%20of%20Proton%20Transfer%20in%20Protonated%20Peptides&rft.jtitle=Journal%20of%20the%20American%20Chemical%20Society&rft.au=Kulh%C3%A1nek,%20Petr&rft.date=2003-11-12&rft.volume=125&rft.issue=45&rft.spage=13678&rft.epage=13679&rft.pages=13678-13679&rft.issn=0002-7863&rft.eissn=1520-5126&rft.coden=JACSAT&rft_id=info:doi/10.1021/ja035800z&rft_dat=%3Cproquest_cross%3E71345481%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-a379t-7096cde1c4945692ef3182e1d6b0cf6260e32163a28184e0cdb0369f841d422c3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=71345481&rft_id=info:pmid/14599203&rfr_iscdi=true