X‐ray structures of aza‐proline‐containing peptides
Identifieur interne : 000838 ( Istex/Corpus ); précédent : 000837; suivant : 000839X‐ray structures of aza‐proline‐containing peptides
Auteurs : Claude Didierjean ; Valerio Del Duca ; Ettore Benedetti ; André Aubry ; Mohamed Zouikri ; Michel Marraud ; Guy BoussardSource :
- The Journal of Peptide Research [ 1397-002X ] ; 1997-12.
English descriptors
- KwdEn :
- Absolute configuration, Acta crystallogr, Amide, Amide bond, Amide groups, Aubry, Azaa, Azpda, Azpla, Azpro, Azpro moiety, Azpro nitrogens, Azpro peptides, Azpro pyrazolidine ring, Azpro residue, Bond angles, Carbon atoms, Chem, Conformation, Crystal structures, Cyclic structure, Electronic conjugation, Hydrogen atoms, Independent molecules, Nitrogen atom, Nitrogen atoms, Peptide, Perkin trans, Present work, Proline, Proline residues, Pyrazolidine, Pyrazolidine ring, Pyrrolidine ring, Standard peptide bond, Sterical hindrances, Structural properties, Symmetrical families, Torsional, Torsional angles, Trans conformation.
- Teeft :
- Absolute configuration, Acta crystallogr, Amide, Amide bond, Amide groups, Aubry, Azaa, Azpda, Azpla, Azpro, Azpro moiety, Azpro nitrogens, Azpro peptides, Azpro pyrazolidine ring, Azpro residue, Bond angles, Carbon atoms, Chem, Conformation, Crystal structures, Cyclic structure, Electronic conjugation, Hydrogen atoms, Independent molecules, Nitrogen atom, Nitrogen atoms, Peptide, Perkin trans, Present work, Proline, Proline residues, Pyrazolidine, Pyrazolidine ring, Pyrrolidine ring, Standard peptide bond, Sterical hindrances, Structural properties, Symmetrical families, Torsional, Torsional angles, Trans conformation.
Abstract
The aza‐analogue of proline (AzPro) contains a nitrogen atom in place of the CHα of the cognate residue. The resolution of the crystal structures of seven AzPro‐containing peptides, presenting a set of ten AzPro motifs, reveals the structural properties of this particular aza‐residue. Because of sterical hindrances, both nitrogen atoms are out of planarity, and the reduced electronic conjugation in the two AzPro‐adjacent amide groups probably explains the longer amide bond distances and the weak proton‐accepting character of the two pyrazolidine nitrogens. The absolute configuration of both AzPro nitrogens depends on the chemical nature of the sequence. In all cases, the AzPro residue assumes the same intrinsic three‐dimensional structure and presents folding tendencies opposed to those induced by proline.
Url:
DOI: 10.1111/j.1399-3011.1997.tb01208.x
Links to Exploration step
ISTEX:84EF0FFB1988184A0DD6229A0EF96EDD1DF8B331Le document en format XML
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Aubry LCM3B, Université Henri Poincaré BP 239, Boulevard des Aiguillettes 54509 Vandœuvre les Nancy Cedex France Tel: +33 383 91 22 62 Fax: +33 383 40 64 92 E‐mail: aubry@lcm3b.u‐nancy.fr</mods:affiliation></affiliation></author><author><name sortKey="Zouikri, Mohamed" sort="Zouikri, Mohamed" uniqKey="Zouikri M" first="Mohamed" last="Zouikri">Mohamed Zouikri</name><affiliation><mods:affiliation>LCPM, CNRS‐URA‐494, ENSIC‐INPL, Nancy, France</mods:affiliation></affiliation><affiliation><mods:affiliation>LCM3B, CNRS‐URA‐809, University Henri Poincaré, Vandœuvre les Nancy, France</mods:affiliation></affiliation></author><author><name sortKey="Marraud, Michel" sort="Marraud, Michel" uniqKey="Marraud M" first="Michel" last="Marraud">Michel Marraud</name><affiliation><mods:affiliation>LCPM, CNRS‐URA‐494, ENSIC‐INPL, Nancy, France</mods:affiliation></affiliation><affiliation><mods:affiliation>LCM3B, CNRS‐URA‐809, University Henri Poincaré, Vandœuvre les Nancy, France</mods:affiliation></affiliation></author><author><name sortKey="Boussard, Guy" sort="Boussard, Guy" uniqKey="Boussard G" first="Guy" last="Boussard">Guy Boussard</name><affiliation><mods:affiliation>LCPM, CNRS‐URA‐494, ENSIC‐INPL, Nancy, France</mods:affiliation></affiliation><affiliation><mods:affiliation>LCM3B, CNRS‐URA‐809, University Henri Poincaré, Vandœuvre les Nancy, France</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">The Journal of Peptide Research</title><title level="j" type="alt">JOURNAL OF PEPTIDE RESEARCH</title><idno type="ISSN">1397-002X</idno><idno type="eISSN">1399-3011</idno><imprint><biblScope unit="vol">50</biblScope><biblScope unit="issue">6</biblScope><biblScope unit="page" from="451">451</biblScope><biblScope unit="page" to="457">457</biblScope><biblScope unit="page-count">7</biblScope><publisher>Blackwell Publishing Ltd</publisher><pubPlace>Oxford, UK</pubPlace><date type="published" when="1997-12">1997-12</date></imprint><idno type="ISSN">1397-002X</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">1397-002X</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Absolute configuration</term><term>Acta crystallogr</term><term>Amide</term><term>Amide bond</term><term>Amide groups</term><term>Aubry</term><term>Azaa</term><term>Azpda</term><term>Azpla</term><term>Azpro</term><term>Azpro moiety</term><term>Azpro nitrogens</term><term>Azpro peptides</term><term>Azpro pyrazolidine ring</term><term>Azpro residue</term><term>Bond angles</term><term>Carbon atoms</term><term>Chem</term><term>Conformation</term><term>Crystal structures</term><term>Cyclic structure</term><term>Electronic conjugation</term><term>Hydrogen atoms</term><term>Independent molecules</term><term>Nitrogen atom</term><term>Nitrogen atoms</term><term>Peptide</term><term>Perkin trans</term><term>Present work</term><term>Proline</term><term>Proline residues</term><term>Pyrazolidine</term><term>Pyrazolidine ring</term><term>Pyrrolidine ring</term><term>Standard peptide bond</term><term>Sterical hindrances</term><term>Structural properties</term><term>Symmetrical families</term><term>Torsional</term><term>Torsional angles</term><term>Trans conformation</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Absolute configuration</term><term>Acta crystallogr</term><term>Amide</term><term>Amide bond</term><term>Amide groups</term><term>Aubry</term><term>Azaa</term><term>Azpda</term><term>Azpla</term><term>Azpro</term><term>Azpro moiety</term><term>Azpro nitrogens</term><term>Azpro peptides</term><term>Azpro pyrazolidine ring</term><term>Azpro residue</term><term>Bond angles</term><term>Carbon atoms</term><term>Chem</term><term>Conformation</term><term>Crystal structures</term><term>Cyclic structure</term><term>Electronic conjugation</term><term>Hydrogen atoms</term><term>Independent molecules</term><term>Nitrogen atom</term><term>Nitrogen atoms</term><term>Peptide</term><term>Perkin trans</term><term>Present work</term><term>Proline</term><term>Proline residues</term><term>Pyrazolidine</term><term>Pyrazolidine ring</term><term>Pyrrolidine ring</term><term>Standard peptide bond</term><term>Sterical hindrances</term><term>Structural properties</term><term>Symmetrical families</term><term>Torsional</term><term>Torsional angles</term><term>Trans conformation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The aza‐analogue of proline (AzPro) contains a nitrogen atom in place of the CHα of the cognate residue. The resolution of the crystal structures of seven AzPro‐containing peptides, presenting a set of ten AzPro motifs, reveals the structural properties of this particular aza‐residue. Because of sterical hindrances, both nitrogen atoms are out of planarity, and the reduced electronic conjugation in the two AzPro‐adjacent amide groups probably explains the longer amide bond distances and the weak proton‐accepting character of the two pyrazolidine nitrogens. The absolute configuration of both AzPro nitrogens depends on the chemical nature of the sequence. In all cases, the AzPro residue assumes the same intrinsic three‐dimensional structure and presents folding tendencies opposed to those induced by proline.</div></front></TEI><istex><corpusName>wiley</corpusName><keywords><teeft><json:string>azpro</json:string><json:string>chem</json:string><json:string>azpla</json:string><json:string>proline</json:string><json:string>azpro residue</json:string><json:string>azpda</json:string><json:string>azaa</json:string><json:string>pyrazolidine</json:string><json:string>peptide</json:string><json:string>torsional</json:string><json:string>amide</json:string><json:string>aubry</json:string><json:string>conformation</json:string><json:string>crystal structures</json:string><json:string>pyrazolidine ring</json:string><json:string>azpro moiety</json:string><json:string>independent molecules</json:string><json:string>perkin trans</json:string><json:string>nitrogen atoms</json:string><json:string>azpro pyrazolidine ring</json:string><json:string>amide bond</json:string><json:string>electronic conjugation</json:string><json:string>azpro peptides</json:string><json:string>sterical hindrances</json:string><json:string>standard peptide bond</json:string><json:string>nitrogen atom</json:string><json:string>acta crystallogr</json:string><json:string>structural properties</json:string><json:string>amide groups</json:string><json:string>torsional angles</json:string><json:string>absolute configuration</json:string><json:string>pyrrolidine ring</json:string><json:string>present work</json:string><json:string>symmetrical families</json:string><json:string>carbon atoms</json:string><json:string>trans conformation</json:string><json:string>azpro nitrogens</json:string><json:string>cyclic structure</json:string><json:string>hydrogen atoms</json:string><json:string>proline residues</json:string><json:string>bond angles</json:string></teeft></keywords><author><json:item><name>CLAUDE DIDIERJEAN</name><affiliations><json:string>LCM3B, CNRS‐URA‐809, University Henri Poincaré, Vandœuvre les Nancy, France</json:string></affiliations></json:item><json:item><name>VALERIO DEL DUCA</name><affiliations><json:string>LCM3B, CNRS‐URA‐809, University Henri Poincaré, Vandœuvre les Nancy, France</json:string></affiliations></json:item><json:item><name>ETTORE BENEDETTI</name><affiliations><json:string>BRC, CNR, University of Napoli Fédérico II, Naples, Italy</json:string><json:string>LCM3B, CNRS‐URA‐809, University Henri Poincaré, Vandœuvre les Nancy, France</json:string></affiliations></json:item><json:item><name>ANDRÉ AUBRY</name><affiliations><json:string>LCM3B, CNRS‐URA‐809, University Henri Poincaré, Vandœuvre les Nancy, France</json:string><json:string>Address: Dr. A. Aubry LCM3B, Université Henri Poincaré BP 239, Boulevard des Aiguillettes 54509 Vandœuvre les Nancy Cedex France Tel: +33 383 91 22 62 Fax: +33 383 40 64 92 E‐mail: aubry@lcm3b.u‐nancy.fr</json:string></affiliations></json:item><json:item><name>MOHAMED ZOUIKRI</name><affiliations><json:string>LCPM, CNRS‐URA‐494, ENSIC‐INPL, Nancy, France</json:string><json:string>LCM3B, CNRS‐URA‐809, University Henri Poincaré, Vandœuvre les Nancy, France</json:string></affiliations></json:item><json:item><name>MICHEL MARRAUD</name><affiliations><json:string>LCPM, CNRS‐URA‐494, ENSIC‐INPL, Nancy, France</json:string><json:string>LCM3B, CNRS‐URA‐809, University Henri Poincaré, Vandœuvre les Nancy, France</json:string></affiliations></json:item><json:item><name>GUY BOUSSARD</name><affiliations><json:string>LCPM, CNRS‐URA‐494, ENSIC‐INPL, Nancy, France</json:string><json:string>LCM3B, CNRS‐URA‐809, University Henri Poincaré, Vandœuvre les Nancy, France</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>aza‐peptide folding</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>aza‐peptides</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>aza‐proline</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>βVI‐turn</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>X‐ray structure</value></json:item></subject><articleId><json:string>CBDD451</json:string></articleId><language><json:string>eng</json:string></language><originalGenre><json:string>article</json:string></originalGenre><abstract>The aza‐analogue of proline (AzPro) contains a nitrogen atom in place of the CHα of the cognate residue. The resolution of the crystal structures of seven AzPro‐containing peptides, presenting a set of ten AzPro motifs, reveals the structural properties of this particular aza‐residue. Because of sterical hindrances, both nitrogen atoms are out of planarity, and the reduced electronic conjugation in the two AzPro‐adjacent amide groups probably explains the longer amide bond distances and the weak proton‐accepting character of the two pyrazolidine nitrogens. The absolute configuration of both AzPro nitrogens depends on the chemical nature of the sequence. In all cases, the AzPro residue assumes the same intrinsic three‐dimensional structure and presents folding tendencies opposed to those induced by proline.</abstract><qualityIndicators><score>5.255</score><pdfVersion>1.4</pdfVersion><pdfPageSize>612 x 792 pts (letter)</pdfPageSize><refBibsNative>true</refBibsNative><abstractCharCount>817</abstractCharCount><pdfWordCount>3327</pdfWordCount><pdfCharCount>21141</pdfCharCount><pdfPageCount>7</pdfPageCount><abstractWordCount>119</abstractWordCount></qualityIndicators><title>X‐ray structures of aza‐proline‐containing peptides</title><genre><json:string>article</json:string></genre><host><title>The Journal of Peptide Research</title><language><json:string>unknown</json:string></language><doi><json:string>10.1111/(ISSN)1399-3011</json:string></doi><issn><json:string>1397-002X</json:string></issn><eissn><json:string>1399-3011</json:string></eissn><publisherId><json:string>CBDD</json:string></publisherId><volume>50</volume><issue>6</issue><pages><first>451</first><last>457</last><total>7</total></pages><genre><json:string>journal</json:string></genre></host><categories><wos></wos><scienceMetrix><json:string>health sciences</json:string><json:string>biomedical research</json:string><json:string>biophysics</json:string></scienceMetrix><inist><json:string>sciences appliquees, technologies et medecines</json:string><json:string>sciences biologiques et medicales</json:string><json:string>sciences biologiques fondamentales et appliquees. psychologie</json:string></inist></categories><publicationDate>1997</publicationDate><copyrightDate>1997</copyrightDate><doi><json:string>10.1111/j.1399-3011.1997.tb01208.x</json:string></doi><id>84EF0FFB1988184A0DD6229A0EF96EDD1DF8B331</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/document/84EF0FFB1988184A0DD6229A0EF96EDD1DF8B331/fulltext/pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/document/84EF0FFB1988184A0DD6229A0EF96EDD1DF8B331/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/84EF0FFB1988184A0DD6229A0EF96EDD1DF8B331/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main">X‐ray structures of aza‐proline‐containing peptides</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>Blackwell Publishing Ltd</publisher><pubPlace>Oxford, UK</pubPlace><date type="published" when="1997-12"></date></publicationStmt><notesStmt><note type="content-type" subtype="article" source="article" scheme="https://content-type.data.istex.fr/ark:/67375/XTP-6N5SZHKN-D">article</note><note type="publication-type" subtype="journal" scheme="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</note></notesStmt><sourceDesc><biblStruct type="article"><analytic><title level="a" type="main">X‐ray structures of aza‐proline‐containing peptides</title><author xml:id="author-0000"><persName><forename type="first">CLAUDE</forename><surname>DIDIERJEAN</surname></persName><affiliation>LCM3B, CNRS‐URA‐809, University Henri Poincaré, Vandœuvre les Nancy, France<address><country key="FR"></country></address></affiliation></author><author xml:id="author-0001"><persName><forename type="first">VALERIO DEL</forename><surname>DUCA</surname></persName><affiliation>LCM3B, CNRS‐URA‐809, University Henri Poincaré, Vandœuvre les Nancy, France<address><country key="FR"></country></address></affiliation></author><author xml:id="author-0002"><persName><forename type="first">ETTORE</forename><surname>BENEDETTI</surname></persName><affiliation>BRC, CNR, University of Napoli Fédérico II, Naples, Italy<address><country key="IT"></country></address></affiliation><affiliation>LCM3B, CNRS‐URA‐809, University Henri Poincaré, Vandœuvre les Nancy, France<address><country key="FR"></country></address></affiliation></author><author xml:id="author-0003" role="corresp"><persName><forename type="first">ANDRÉ</forename><surname>AUBRY</surname></persName><affiliation>LCM3B, CNRS‐URA‐809, University Henri Poincaré, Vandœuvre les Nancy, France<address><country key="FR"></country></address></affiliation><affiliation>Address: Dr. A. Aubry LCM3B, Université Henri Poincaré BP 239, Boulevard des Aiguillettes 54509 Vandœuvre les Nancy Cedex France Tel: +33 383 91 22 62 Fax: +33 383 40 64 92 E‐mail: aubry@lcm3b.u‐nancy.fr</affiliation></author><author xml:id="author-0004"><persName><forename type="first">MOHAMED</forename><surname>ZOUIKRI</surname></persName><affiliation>LCPM, CNRS‐URA‐494, ENSIC‐INPL, Nancy, France<address><country key="FR"></country></address></affiliation><affiliation>LCM3B, CNRS‐URA‐809, University Henri Poincaré, Vandœuvre les Nancy, France<address><country key="FR"></country></address></affiliation></author><author xml:id="author-0005"><persName><forename type="first">MICHEL</forename><surname>MARRAUD</surname></persName><affiliation>LCPM, CNRS‐URA‐494, ENSIC‐INPL, Nancy, France<address><country key="FR"></country></address></affiliation><affiliation>LCM3B, CNRS‐URA‐809, University Henri Poincaré, Vandœuvre les Nancy, France<address><country key="FR"></country></address></affiliation></author><author xml:id="author-0006"><persName><forename type="first">GUY</forename><surname>BOUSSARD</surname></persName><affiliation>LCPM, CNRS‐URA‐494, ENSIC‐INPL, Nancy, France<address><country key="FR"></country></address></affiliation><affiliation>LCM3B, CNRS‐URA‐809, University Henri Poincaré, Vandœuvre les Nancy, France<address><country key="FR"></country></address></affiliation></author><idno type="istex">84EF0FFB1988184A0DD6229A0EF96EDD1DF8B331</idno><idno type="ark">ark:/67375/WNG-GQ2NKP6H-Z</idno><idno type="DOI">10.1111/j.1399-3011.1997.tb01208.x</idno><idno type="unit">CBDD451</idno><idno type="toTypesetVersion">file:CBDD.CBDD451.pdf</idno></analytic><monogr><title level="j" type="main">The Journal of Peptide Research</title><title level="j" type="alt">JOURNAL OF PEPTIDE RESEARCH</title><idno type="pISSN">1397-002X</idno><idno type="eISSN">1399-3011</idno><idno type="book-DOI">10.1111/(ISSN)1399-3011</idno><idno type="book-part-DOI">10.1111/jpp.1997.50.issue-6</idno><idno type="product">CBDD</idno><idno type="publisherDivision">ST</idno><imprint><biblScope unit="vol">50</biblScope><biblScope unit="issue">6</biblScope><biblScope unit="page" from="451">451</biblScope><biblScope unit="page" to="457">457</biblScope><biblScope unit="page-count">7</biblScope><publisher>Blackwell Publishing Ltd</publisher><pubPlace>Oxford, UK</pubPlace><date type="published" when="1997-12"></date></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><abstract xml:lang="en" style="main"><p>The aza‐analogue of proline (AzPro) contains a nitrogen atom in place of the CH<hi rend="superscript">α</hi> of the cognate residue. The resolution of the crystal structures of seven AzPro‐containing peptides, presenting a set of ten AzPro motifs, reveals the structural properties of this particular aza‐residue. Because of sterical hindrances, both nitrogen atoms are out of planarity, and the reduced electronic conjugation in the two AzPro‐adjacent amide groups probably explains the longer amide bond distances and the weak proton‐accepting character of the two pyrazolidine nitrogens. The absolute configuration of both AzPro nitrogens depends on the chemical nature of the sequence. In all cases, the AzPro residue assumes the same intrinsic three‐dimensional structure and presents folding tendencies opposed to those induced by proline.</p></abstract><textClass><keywords xml:lang="en"><term xml:id="k1">aza‐peptide folding</term><term xml:id="k2">aza‐peptides</term><term xml:id="k3">aza‐proline</term><term xml:id="k4">βVI‐turn</term><term xml:id="k5">X‐ray structure
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Aubry LCM3B, Université Henri Poincaré BP 239, Boulevard des Aiguillettes 54509 Vandœuvre les Nancy Cedex France Tel: +33 383 91 22 62 Fax: +33 383 40 64 92 E‐mail: aubry@lcm3b.u‐nancy.fr</correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:CBDD.CBDD451.pdf"></link></linkGroup></publicationMeta><contentMeta><unparsedEditorialHistory>Received 9 May, revised 25 June, accepted for publication 10 August 1997</unparsedEditorialHistory><countGroup><count type="referenceTotal" number="46"></count><count type="linksCrossRef" number="12"></count></countGroup><titleGroup><title type="main">X‐ray structures of aza‐proline‐containing peptides</title></titleGroup><creators><creator creatorRole="author" xml:id="cr1" affiliationRef="#a1"><personName><givenNames>CLAUDE</givenNames><familyName>DIDIERJEAN</familyName></personName></creator><creator creatorRole="author" xml:id="cr2" affiliationRef="#a1"><personName><givenNames>VALERIO DEL</givenNames><familyName>DUCA</familyName></personName></creator><creator creatorRole="author" xml:id="cr3" affiliationRef="#a2 #a1"><personName><givenNames>ETTORE</givenNames><familyName>BENEDETTI</familyName></personName></creator><creator creatorRole="author" xml:id="cr4" affiliationRef="#a1" corresponding="yes"><personName><givenNames>ANDRÉ</givenNames><familyName>AUBRY</familyName></personName></creator><creator creatorRole="author" xml:id="cr5" affiliationRef="#a3 #a1"><personName><givenNames>MOHAMED</givenNames><familyName>ZOUIKRI</familyName></personName></creator><creator creatorRole="author" xml:id="cr6" affiliationRef="#a3 #a1"><personName><givenNames>MICHEL</givenNames><familyName>MARRAUD</familyName></personName></creator><creator creatorRole="author" xml:id="cr7" affiliationRef="#a3 #a1"><personName><givenNames>GUY</givenNames><familyName>BOUSSARD</familyName></personName></creator></creators><affiliationGroup><affiliation xml:id="a1" countryCode="FR"><unparsedAffiliation>LCM3B, CNRS‐URA‐809, University Henri Poincaré, Vandœuvre les Nancy, France</unparsedAffiliation></affiliation><affiliation xml:id="a2" countryCode="IT"><unparsedAffiliation>BRC, CNR, University of Napoli Fédérico II, Naples, Italy</unparsedAffiliation></affiliation><affiliation xml:id="a3" countryCode="FR"><unparsedAffiliation>LCPM, CNRS‐URA‐494, ENSIC‐INPL, Nancy, France</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en"><keyword xml:id="k1">aza‐peptide folding</keyword><keyword xml:id="k2">aza‐peptides</keyword><keyword xml:id="k3">aza‐proline</keyword><keyword xml:id="k4">βVI‐turn</keyword><keyword xml:id="k5">X‐ray structure
</keyword></keywordGroup><abstractGroup><abstract type="main" xml:lang="en"><p>The aza‐analogue of proline (AzPro) contains a nitrogen atom in place of the CH<sup>α</sup> of the cognate residue. The resolution of the crystal structures of seven AzPro‐containing peptides, presenting a set of ten AzPro motifs, reveals the structural properties of this particular aza‐residue. Because of sterical hindrances, both nitrogen atoms are out of planarity, and the reduced electronic conjugation in the two AzPro‐adjacent amide groups probably explains the longer amide bond distances and the weak proton‐accepting character of the two pyrazolidine nitrogens. The absolute configuration of both AzPro nitrogens depends on the chemical nature of the sequence. In all cases, the AzPro residue assumes the same intrinsic three‐dimensional structure and presents folding tendencies opposed to those induced by proline.</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>X‐ray structures of aza‐proline‐containing peptides</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>X‐ray structures of aza‐proline‐containing peptides</title></titleInfo><name type="personal"><namePart type="given">CLAUDE</namePart><namePart type="family">DIDIERJEAN</namePart><affiliation>LCM3B, CNRS‐URA‐809, University Henri Poincaré, Vandœuvre les Nancy, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">VALERIO DEL</namePart><namePart type="family">DUCA</namePart><affiliation>LCM3B, CNRS‐URA‐809, University Henri Poincaré, Vandœuvre les Nancy, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">ETTORE</namePart><namePart type="family">BENEDETTI</namePart><affiliation>BRC, CNR, University of Napoli Fédérico II, Naples, Italy</affiliation><affiliation>LCM3B, CNRS‐URA‐809, University Henri Poincaré, Vandœuvre les Nancy, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">ANDRÉ</namePart><namePart type="family">AUBRY</namePart><affiliation>LCM3B, CNRS‐URA‐809, University Henri Poincaré, Vandœuvre les Nancy, France</affiliation><affiliation>Correspondence address: Address: Dr. A. Aubry LCM3B, Université Henri Poincaré BP 239, Boulevard des Aiguillettes 54509 Vandœuvre les Nancy Cedex France Tel: +33 383 91 22 62 Fax: +33 383 40 64 92 E‐mail: aubry@lcm3b.u‐nancy.fr</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">MOHAMED</namePart><namePart type="family">ZOUIKRI</namePart><affiliation>LCPM, CNRS‐URA‐494, ENSIC‐INPL, Nancy, France</affiliation><affiliation>LCM3B, CNRS‐URA‐809, University Henri Poincaré, Vandœuvre les 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>LCPM, CNRS‐URA‐494, ENSIC‐INPL, Nancy, France</affiliation><affiliation>LCM3B, CNRS‐URA‐809, University Henri Poincaré, Vandœuvre les Nancy, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">GUY</namePart><namePart type="family">BOUSSARD</namePart><affiliation>LCPM, CNRS‐URA‐494, ENSIC‐INPL, Nancy, France</affiliation><affiliation>LCM3B, CNRS‐URA‐809, University Henri Poincaré, Vandœuvre les 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">1997-12</dateIssued><edition>Received 9 May, revised 25 June, accepted for publication 10 August 1997</edition><copyrightDate encoding="w3cdtf">1997</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><extent unit="references">46</extent><extent unit="linksCrossRef">12</extent></physicalDescription><abstract lang="en">The aza‐analogue of proline (AzPro) contains a nitrogen atom in place of the CHα of the cognate residue. The resolution of the crystal structures of seven AzPro‐containing peptides, presenting a set of ten AzPro motifs, reveals the structural properties of this particular aza‐residue. Because of sterical hindrances, both nitrogen atoms are out of planarity, and the reduced electronic conjugation in the two AzPro‐adjacent amide groups probably explains the longer amide bond distances and the weak proton‐accepting character of the two pyrazolidine nitrogens. The absolute configuration of both AzPro nitrogens depends on the chemical nature of the sequence. In all cases, the AzPro residue assumes the same intrinsic three‐dimensional structure and presents folding tendencies opposed to those induced by proline.</abstract><subject lang="en"><genre>keywords</genre><topic>aza‐peptide folding</topic><topic>aza‐peptides</topic><topic>aza‐proline</topic><topic>βVI‐turn</topic><topic>X‐ray structure</topic></subject><relatedItem type="host"><titleInfo><title>The Journal of Peptide 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">1397-002X</identifier><identifier type="eISSN">1399-3011</identifier><identifier type="DOI">10.1111/(ISSN)1399-3011</identifier><identifier type="PublisherID">CBDD</identifier><part><date>1997</date><detail type="volume"><caption>vol.</caption><number>50</number></detail><detail type="issue"><caption>no.</caption><number>6</number></detail><extent unit="pages"><start>451</start><end>457</end><total>7</total></extent></part></relatedItem><identifier type="istex">84EF0FFB1988184A0DD6229A0EF96EDD1DF8B331</identifier><identifier type="ark">ark:/67375/WNG-GQ2NKP6H-Z</identifier><identifier type="DOI">10.1111/j.1399-3011.1997.tb01208.x</identifier><identifier type="ArticleID">CBDD451</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/84EF0FFB1988184A0DD6229A0EF96EDD1DF8B331/metadata/json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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