Structural variations in the crystal structures of two homologous DL‐Leu and Δ‐Leu containing peptides
Identifieur interne : 000592 ( Istex/Corpus ); précédent : 000591; suivant : 000593Structural variations in the crystal structures of two homologous DL‐Leu and Δ‐Leu containing peptides
Auteurs : Larbi El-Masdouri ; André Aubry ; Guy Boussard ; Michel MarraudSource :
- International Journal of Peptide and Protein Research [ 0367-8377 ] ; 1992-12.
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Abstract
The similar conformations and interaction modes of Ac‐DL‐Leu‐Nme2 and Ac‐Δ‐Leu‐NMe2 molecules in the solid state allow the comparison of their geometrical parameters. The most evident variations are essentially restricted to the α,β‐unsaturated side‐chain which adopts the Z‐disposition. The dimensions of the peptide backbone are much less sensitive to α,β‐unsaturation, with a small shortening by 0.04 Å and 0.02 Å of the N‐Cα and Cα‐C′ bonds, respectively, and an increase by 6° of the N‐Cα‐ C′ bond angle. The ethylenic and amide groups in the Δ‐Leu derivative are far from coplanarity, and a significant electronic conjugation of the π‐orbital is likely to be rejected.
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DOI: 10.1111/j.1399-3011.1992.tb00431.x
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ISTEX:EAAC3778D92078648424A2FA17BD1C9FFF73C786Le document en format XML
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The most evident variations are essentially restricted to the α,β‐unsaturated side‐chain which adopts the Z‐disposition. The dimensions of the peptide backbone are much less sensitive to α,β‐unsaturation, with a small shortening by 0.04 Å and 0.02 Å of the N‐Cα and Cα‐C′ bonds, respectively, and an increase by 6° of the N‐Cα‐ C′ bond angle. The ethylenic and amide groups in the Δ‐Leu derivative are far from coplanarity, and a significant electronic conjugation of the π‐orbital is likely to be rejected.</div></front></TEI><istex><corpusName>wiley</corpusName><keywords><teeft><json:string>peptide</json:string><json:string>electronic conjugation</json:string><json:string>aubry</json:string><json:string>dihedral</json:string><json:string>chauhan</json:string><json:string>marraud</json:string><json:string>narula</json:string><json:string>pprn</json:string><json:string>singh</json:string><json:string>similar conformations</json:string><json:string>derivative</json:string><json:string>conjugation</json:string><json:string>peptide backbone</json:string><json:string>interaction modes</json:string><json:string>hydrogen bond</json:string><json:string>cyclic dimers</json:string><json:string>geometrical parameters</json:string><json:string>crystal structures</json:string><json:string>amide groups</json:string><json:string>nonhydrogen atoms</json:string></teeft></keywords><author><json:item><name>LARBI EL‐MASDOURI</name><affiliations><json:string>URA‐CNRS‐809, University of Nancy</json:string></affiliations></json:item><json:item><name>ANDRÉ AUBRY</name><affiliations><json:string>URA‐CNRS‐809, University of Nancy</json:string></affiliations></json:item><json:item><name>GUY BOUSSARD</name><affiliations><json:string>URA‐CNRS‐494. 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The dimensions of the peptide backbone are much less sensitive to α,β‐unsaturation, with a small shortening by 0.04 Å and 0.02 Å of the N‐Cα and Cα‐C′ bonds, respectively, and an increase by 6° of the N‐Cα‐ C′ bond angle. 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ENSIC‐INPL, Nancy, France<address><country key="FR"></country></address></affiliation><affiliation>Address: Dr G. Boussard LCPM‐ENSIC, BP 451 54001 Nancy, France</affiliation></author><author xml:id="author-0003"><persName><forename type="first">MICHEL</forename><surname>MARRAUD</surname></persName><affiliation>URA‐CNRS‐494. 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The most evident variations are essentially restricted to the α,β‐unsaturated side‐chain which adopts the Z‐disposition. The dimensions of the peptide backbone are much less sensitive to α,β‐unsaturation, with a small shortening by 0.04 Å and 0.02 Å of the N‐C<hi rend="superscript">α</hi> and C<hi rend="superscript">α</hi>‐C′ bonds, respectively, and an increase by 6° of the N‐C<hi rend="superscript">α</hi>‐ C′ bond angle. The ethylenic and amide groups in the Δ‐Leu derivative are far from coplanarity, and a significant electronic conjugation of the π‐orbital is likely to be rejected.</p></abstract><textClass><keywords xml:lang="en"><term xml:id="k1">crystal molecular structure</term><term xml:id="k2">dehydroleucine derivative</term><term xml:id="k3">dehydro peptides</term><term xml:id="k4">X‐ray diffraction</term></keywords></textClass><langUsage><language ident="en"></language></langUsage></profileDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/document/EAAC3778D92078648424A2FA17BD1C9FFF73C786/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Wiley, elements deleted: body"><istex:xmlDeclaration>version="1.0" encoding="UTF-8" standalone="yes"</istex:xmlDeclaration><istex:document><component version="2.0" type="serialArticle" xml:lang="en"><header><publicationMeta level="product"><publisherInfo><publisherName>Blackwell Publishing Ltd</publisherName><publisherLoc>Oxford, UK</publisherLoc></publisherInfo><doi origin="wiley" registered="yes">10.1111/(ISSN)1399-3011a</doi><issn type="print">0367-8377</issn><issn type="electronic">1399-3011</issn><idGroup><id type="product" value="CBDD"></id><id type="publisherDivision" value="ST"></id></idGroup><titleGroup><title type="main" sort="INTERNATIONAL JOURNAL OF PEPTIDE AND PROTEIN RESEARCH">International Journal of Peptide and Protein Research</title></titleGroup></publicationMeta><publicationMeta level="part" position="12006"><doi origin="wiley">10.1111/jpp.1992.40.issue-6</doi><numberingGroup><numbering type="journalVolume" number="40">40</numbering><numbering type="journalIssue" number="6">6</numbering></numberingGroup><coverDate startDate="1992-12">December 1992</coverDate></publicationMeta><publicationMeta level="unit" type="article" position="0048200" status="forIssue"><doi origin="wiley">10.1111/j.1399-3011.1992.tb00431.x</doi><idGroup><id type="unit" value="CBDD482"></id></idGroup><countGroup><count type="pageTotal" number="5"></count></countGroup><eventGroup><event type="firstOnline" date="2009-01-12"></event><event type="publishedOnlineFinalForm" date="2009-01-12"></event><event type="xmlConverted" agent="Converter:BPG_TO_WML3G version:2.3.5 mode:FullText source:HeaderRef result:HeaderRef" date="2010-04-07"></event><event type="xmlConverted" agent="Converter:WILEY_ML3G_TO_WILEY_ML3GV2 version:3.8.8" date="2014-01-08"></event><event type="xmlConverted" agent="Converter:WML3G_To_WML3G version:4.1.7 mode:FullText,remove_FC" date="2014-10-24"></event></eventGroup><numberingGroup><numbering type="pageFirst" number="482">482</numbering><numbering type="pageLast" number="486">486</numbering></numberingGroup><correspondenceTo>Address: Dr G. Boussard LCPM‐ENSIC, BP 451 54001 Nancy, France</correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:CBDD.CBDD482.pdf"></link></linkGroup></publicationMeta><contentMeta><unparsedEditorialHistory>Received 2 December 1991, accepted for publication 20 March 1992</unparsedEditorialHistory><countGroup><count type="referenceTotal" number="18"></count><count type="linksCrossRef" number="6"></count></countGroup><titleGroup><title type="main">Structural variations in the crystal structures of two homologous DL‐Leu and Δ‐Leu containing peptides<link href="#fn1"><sup>+</sup></link></title></titleGroup><creators><creator creatorRole="author" xml:id="cr1" affiliationRef="#a1"><personName><givenNames>LARBI</givenNames><familyName>EL‐MASDOURI</familyName></personName></creator><creator creatorRole="author" xml:id="cr2" affiliationRef="#a1"><personName><givenNames>ANDRÉ</givenNames><familyName>AUBRY</familyName></personName></creator><creator creatorRole="author" xml:id="cr3" affiliationRef="#a2" corresponding="yes"><personName><givenNames>GUY</givenNames><familyName>BOUSSARD</familyName></personName></creator><creator creatorRole="author" xml:id="cr4" affiliationRef="#a2"><personName><givenNames>MICHEL</givenNames><familyName>MARRAUD</familyName></personName></creator></creators><affiliationGroup><affiliation xml:id="a1"><unparsedAffiliation>URA‐CNRS‐809, University of Nancy</unparsedAffiliation></affiliation><affiliation xml:id="a2" countryCode="FR"><unparsedAffiliation>URA‐CNRS‐494. ENSIC‐INPL, Nancy, France</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en"><keyword xml:id="k1">crystal molecular structure</keyword><keyword xml:id="k2">dehydroleucine derivative</keyword><keyword xml:id="k3">dehydro peptides</keyword><keyword xml:id="k4">X‐ray diffraction</keyword></keywordGroup><abstractGroup><abstract type="main" xml:lang="en"><p>The similar conformations and interaction modes of Ac‐DL‐Leu‐Nme<sub>2</sub> and Ac‐Δ‐Leu‐NMe<sub>2</sub> molecules in the solid state allow the comparison of their geometrical parameters. The most evident variations are essentially restricted to the α,β‐unsaturated side‐chain which adopts the Z‐disposition. The dimensions of the peptide backbone are much less sensitive to α,β‐unsaturation, with a small shortening by 0.04 Å and 0.02 Å of the N‐C<sup>α</sup> and C<sup>α</sup>‐C′ bonds, respectively, and an increase by 6° of the N‐C<sup>α</sup>‐ C′ bond angle. The ethylenic and amide groups in the Δ‐Leu derivative are far from coplanarity, and a significant electronic conjugation of the π‐orbital is likely to be rejected.</p></abstract></abstractGroup></contentMeta><noteGroup><note xml:id="fn1"><label><sup>+</sup></label><p>Contribution of the Laboratory of Molecular Processes, Nancy.</p></note></noteGroup></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Structural variations in the crystal structures of two homologous DL‐Leu and Δ‐Leu containing peptides</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Structural variations in the crystal structures of two homologous DL‐Leu and Δ‐Leu containing peptides+</title></titleInfo><name type="personal"><namePart type="given">LARBI</namePart><namePart type="family">EL‐MASDOURI</namePart><affiliation>URA‐CNRS‐809, University of Nancy</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">ANDRÉ</namePart><namePart type="family">AUBRY</namePart><affiliation>URA‐CNRS‐809, University of Nancy</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">GUY</namePart><namePart type="family">BOUSSARD</namePart><affiliation>URA‐CNRS‐494. ENSIC‐INPL, Nancy, France</affiliation><affiliation>Correspondence address: Address: Dr G. Boussard LCPM‐ENSIC, BP 451 54001 Nancy, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">MICHEL</namePart><namePart type="family">MARRAUD</namePart><affiliation>URA‐CNRS‐494. ENSIC‐INPL, Nancy, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-6N5SZHKN-D">article</genre><originInfo><publisher>Blackwell Publishing Ltd</publisher><place><placeTerm type="text">Oxford, UK</placeTerm></place><dateIssued encoding="w3cdtf">1992-12</dateIssued><edition>Received 2 December 1991, accepted for publication 20 March 1992</edition><copyrightDate encoding="w3cdtf">1992</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><extent unit="references">18</extent><extent unit="linksCrossRef">6</extent></physicalDescription><abstract lang="en">The similar conformations and interaction modes of Ac‐DL‐Leu‐Nme2 and Ac‐Δ‐Leu‐NMe2 molecules in the solid state allow the comparison of their geometrical parameters. The most evident variations are essentially restricted to the α,β‐unsaturated side‐chain which adopts the Z‐disposition. The dimensions of the peptide backbone are much less sensitive to α,β‐unsaturation, with a small shortening by 0.04 Å and 0.02 Å of the N‐Cα and Cα‐C′ bonds, respectively, and an increase by 6° of the N‐Cα‐ C′ bond angle. The ethylenic and amide groups in the Δ‐Leu derivative are far from coplanarity, and a significant electronic conjugation of the π‐orbital is likely to be rejected.</abstract><note type="content">*Contribution of the Laboratory of Molecular Processes, Nancy.</note><subject lang="en"><genre>keywords</genre><topic>crystal molecular structure</topic><topic>dehydroleucine derivative</topic><topic>dehydro peptides</topic><topic>X‐ray diffraction</topic></subject><relatedItem type="host"><titleInfo><title>International Journal of Peptide and Protein Research</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><identifier type="ISSN">0367-8377</identifier><identifier type="eISSN">1399-3011</identifier><identifier type="DOI">10.1111/(ISSN)1399-3011a</identifier><identifier type="PublisherID">CBDD</identifier><part><date>1992</date><detail type="volume"><caption>vol.</caption><number>40</number></detail><detail type="issue"><caption>no.</caption><number>6</number></detail><extent unit="pages"><start>482</start><end>486</end><total>5</total></extent></part></relatedItem><identifier type="istex">EAAC3778D92078648424A2FA17BD1C9FFF73C786</identifier><identifier type="ark">ark:/67375/WNG-W01B542S-T</identifier><identifier type="DOI">10.1111/j.1399-3011.1992.tb00431.x</identifier><identifier type="ArticleID">CBDD482</identifier><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-L0C46X92-X">wiley</recordContentSource><recordOrigin>Blackwell Publishing Ltd</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/document/EAAC3778D92078648424A2FA17BD1C9FFF73C786/metadata/json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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|texte= Structural variations in the crystal structures of two homologous DL‐Leu and Δ‐Leu containing peptides
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