Aza‐peptides. III. Experimental structural analysis of aza‐alanme and aza‐asparagine‐containing peptides
Identifieur interne : 000623 ( Istex/Corpus ); précédent : 000622; suivant : 000624Aza‐peptides. III. Experimental structural analysis of aza‐alanme and aza‐asparagine‐containing peptides
Auteurs : Frédéric André ; André Vicherat ; Guy Boussard ; André Aubry ; Michel MarraudSource :
- The Journal of Peptide Research [ 1397-002X ] ; 1997-11.
English descriptors
- KwdEn :
- Amide, Amide bond, Amide group, Amide protons, Amino acid residue, Aubry, Azala, Azasn, Azasn carboxamide, Azasn derivatives, Azasn residue, Azasp, Azxaa, Azxaa component, Biopolymers pept, Boussard, Bruker apparatus, Chem, Chemical shift variation, Cognate peptides, Conformational properties, Consensus sequence, Crystal structure, Dmso, Gravity silica, High wave number contribution, Hydrazino, Hydrazino peptides, Hydrogen bond, Intramolecular hydrogen bond, Intramolecular interaction, Lone pair, Main torsional angles, Marraud, Mmol, Other hand, Pept, Peptide, Perkin trans, Previous studies, Proton, Proton donor, Proton resonance, Room temperature, Solvent sensitivity, Tertiary amide, Vibrator, Wave number azasn absorption.
- Teeft :
- Amide, Amide bond, Amide group, Amide protons, Amino acid residue, Aubry, Azala, Azasn, Azasn carboxamide, Azasn derivatives, Azasn residue, Azasp, Azxaa, Azxaa component, Biopolymers pept, Boussard, Bruker apparatus, Chem, Chemical shift variation, Cognate peptides, Conformational properties, Consensus sequence, Crystal structure, Dmso, Gravity silica, High wave number contribution, Hydrazino, Hydrazino peptides, Hydrogen bond, Intramolecular hydrogen bond, Intramolecular interaction, Lone pair, Main torsional angles, Marraud, Mmol, Other hand, Pept, Peptide, Perkin trans, Previous studies, Proton, Proton donor, Proton resonance, Room temperature, Solvent sensitivity, Tertiary amide, Vibrator, Wave number azasn absorption.
Abstract
To determine the structural perturbations induced by the CαH→Nα exchange in aza‐peptides, we have examined by H NMR and IR spectroscopy various derivatives of the aza‐analogues of alanine, aspartic acid and asparagine in different organic solvents with increasing polarity. Their general formulas are: R'‐AzXaa‐NR2R3, R'‐Pro‐AzXaa‐NR2R3 and R‐AzXaa‐Pro‐NR2R3 (where AzXaa denotes the aza‐analogue of the amino acid residue Xaa = Ala, Asp, Asn; R = Boc, Z; R2, R3= H, Me, iPr). The aza‐analogue of an amino acid residue appears to be a strong p‐turn‐inducing motif, and the AzAsn carboxamide side‐chain is capable of interacting, as a proton donor, with the preceding peptide carbonyl group.
Url:
DOI: 10.1111/j.1399-3011.1997.tb01197.x
Links to Exploration step
ISTEX:61BD6B420D447C2DBB69BCCF8819B7965C87087ALe document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Aza‐peptides. III. Experimental structural analysis of aza‐alanme and aza‐asparagine‐containing peptides</title><author><name sortKey="Andre, Frederic" sort="Andre, Frederic" uniqKey="Andre F" first="Frédéric" last="André">Frédéric André</name><affiliation><mods:affiliation>LCPM, CNRS‐URA‐494, ENSIC‐INPL, Nancy, France, and</mods:affiliation></affiliation></author><author><name sortKey="Vicherat, Andre" sort="Vicherat, Andre" uniqKey="Vicherat A" first="André" last="Vicherat">André Vicherat</name><affiliation><mods:affiliation>LCPM, CNRS‐URA‐494, ENSIC‐INPL, Nancy, France, and</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, and</mods:affiliation></affiliation><affiliation><mods:affiliation>Correspondence address: Address: Dr. G. Boussard LCPM, ENSIC‐INPL BP451, 1 rue Grandville 54001 Nancy Cedex France Phone:+33 383 1751 96 Fax: +33 383 37 99 77 E‐mail: boussard@lcpm.ensic.u‐nancy.fr</mods:affiliation></affiliation></author><author><name sortKey="Aubry, Andre" sort="Aubry, Andre" uniqKey="Aubry A" first="André" last="Aubry">André Aubry</name><affiliation><mods:affiliation>LCM3B, CNRS‐URA‐809, University Henri Poincaré, Vandazuvre, 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, and</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:61BD6B420D447C2DBB69BCCF8819B7965C87087A</idno><date when="1997" year="1997">1997</date><idno type="doi">10.1111/j.1399-3011.1997.tb01197.x</idno><idno type="url">https://api.istex.fr/document/61BD6B420D447C2DBB69BCCF8819B7965C87087A/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">000623</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">000623</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main">Aza‐peptides. III. Experimental structural analysis of aza‐alanme and aza‐asparagine‐containing peptides</title><author><name sortKey="Andre, Frederic" sort="Andre, Frederic" uniqKey="Andre F" first="Frédéric" last="André">Frédéric André</name><affiliation><mods:affiliation>LCPM, CNRS‐URA‐494, ENSIC‐INPL, Nancy, France, and</mods:affiliation></affiliation></author><author><name sortKey="Vicherat, Andre" sort="Vicherat, Andre" uniqKey="Vicherat A" first="André" last="Vicherat">André Vicherat</name><affiliation><mods:affiliation>LCPM, CNRS‐URA‐494, ENSIC‐INPL, Nancy, France, and</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, and</mods:affiliation></affiliation><affiliation><mods:affiliation>Correspondence address: Address: Dr. G. Boussard LCPM, ENSIC‐INPL BP451, 1 rue Grandville 54001 Nancy Cedex France Phone:+33 383 1751 96 Fax: +33 383 37 99 77 E‐mail: boussard@lcpm.ensic.u‐nancy.fr</mods:affiliation></affiliation></author><author><name sortKey="Aubry, Andre" sort="Aubry, Andre" uniqKey="Aubry A" first="André" last="Aubry">André Aubry</name><affiliation><mods:affiliation>LCM3B, CNRS‐URA‐809, University Henri Poincaré, Vandazuvre, 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, and</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">5</biblScope><biblScope unit="page" from="372">372</biblScope><biblScope unit="page" to="381">381</biblScope><biblScope unit="page-count">10</biblScope><publisher>Blackwell Publishing Ltd</publisher><pubPlace>Oxford, UK</pubPlace><date type="published" when="1997-11">1997-11</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>Amide</term><term>Amide bond</term><term>Amide group</term><term>Amide protons</term><term>Amino acid residue</term><term>Aubry</term><term>Azala</term><term>Azasn</term><term>Azasn carboxamide</term><term>Azasn derivatives</term><term>Azasn residue</term><term>Azasp</term><term>Azxaa</term><term>Azxaa component</term><term>Biopolymers pept</term><term>Boussard</term><term>Bruker apparatus</term><term>Chem</term><term>Chemical shift variation</term><term>Cognate peptides</term><term>Conformational properties</term><term>Consensus sequence</term><term>Crystal structure</term><term>Dmso</term><term>Gravity silica</term><term>High wave number contribution</term><term>Hydrazino</term><term>Hydrazino peptides</term><term>Hydrogen bond</term><term>Intramolecular hydrogen bond</term><term>Intramolecular interaction</term><term>Lone pair</term><term>Main torsional angles</term><term>Marraud</term><term>Mmol</term><term>Other hand</term><term>Pept</term><term>Peptide</term><term>Perkin trans</term><term>Previous studies</term><term>Proton</term><term>Proton donor</term><term>Proton resonance</term><term>Room temperature</term><term>Solvent sensitivity</term><term>Tertiary amide</term><term>Vibrator</term><term>Wave number azasn absorption</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Amide</term><term>Amide bond</term><term>Amide group</term><term>Amide protons</term><term>Amino acid residue</term><term>Aubry</term><term>Azala</term><term>Azasn</term><term>Azasn carboxamide</term><term>Azasn derivatives</term><term>Azasn residue</term><term>Azasp</term><term>Azxaa</term><term>Azxaa component</term><term>Biopolymers pept</term><term>Boussard</term><term>Bruker apparatus</term><term>Chem</term><term>Chemical shift variation</term><term>Cognate peptides</term><term>Conformational properties</term><term>Consensus sequence</term><term>Crystal structure</term><term>Dmso</term><term>Gravity silica</term><term>High wave number contribution</term><term>Hydrazino</term><term>Hydrazino peptides</term><term>Hydrogen bond</term><term>Intramolecular hydrogen bond</term><term>Intramolecular interaction</term><term>Lone pair</term><term>Main torsional angles</term><term>Marraud</term><term>Mmol</term><term>Other hand</term><term>Pept</term><term>Peptide</term><term>Perkin trans</term><term>Previous studies</term><term>Proton</term><term>Proton donor</term><term>Proton resonance</term><term>Room temperature</term><term>Solvent sensitivity</term><term>Tertiary amide</term><term>Vibrator</term><term>Wave number azasn absorption</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">To determine the structural perturbations induced by the CαH→Nα exchange in aza‐peptides, we have examined by H NMR and IR spectroscopy various derivatives of the aza‐analogues of alanine, aspartic acid and asparagine in different organic solvents with increasing polarity. Their general formulas are: R'‐AzXaa‐NR2R3, R'‐Pro‐AzXaa‐NR2R3 and R‐AzXaa‐Pro‐NR2R3 (where AzXaa denotes the aza‐analogue of the amino acid residue Xaa = Ala, Asp, Asn; R = Boc, Z; R2, R3= H, Me, iPr). The aza‐analogue of an amino acid residue appears to be a strong p‐turn‐inducing motif, and the AzAsn carboxamide side‐chain is capable of interacting, as a proton donor, with the preceding peptide carbonyl group.</div></front></TEI><istex><corpusName>wiley</corpusName><keywords><teeft><json:string>azasn</json:string><json:string>azxaa</json:string><json:string>marraud</json:string><json:string>hydrazino</json:string><json:string>mmol</json:string><json:string>aubry</json:string><json:string>boussard</json:string><json:string>azala</json:string><json:string>peptide</json:string><json:string>amide</json:string><json:string>pept</json:string><json:string>vibrator</json:string><json:string>chem</json:string><json:string>azasp</json:string><json:string>crystal structure</json:string><json:string>dmso</json:string><json:string>hydrogen bond</json:string><json:string>hydrazino peptides</json:string><json:string>chemical shift variation</json:string><json:string>gravity silica</json:string><json:string>proton donor</json:string><json:string>proton resonance</json:string><json:string>amino acid residue</json:string><json:string>proton</json:string><json:string>room temperature</json:string><json:string>tertiary amide</json:string><json:string>amide protons</json:string><json:string>high wave number contribution</json:string><json:string>intramolecular interaction</json:string><json:string>azasn derivatives</json:string><json:string>azxaa component</json:string><json:string>consensus sequence</json:string><json:string>wave number azasn absorption</json:string><json:string>bruker apparatus</json:string><json:string>lone pair</json:string><json:string>azasn residue</json:string><json:string>main torsional angles</json:string><json:string>conformational properties</json:string><json:string>solvent sensitivity</json:string><json:string>previous studies</json:string><json:string>amide bond</json:string><json:string>other hand</json:string><json:string>cognate peptides</json:string><json:string>amide group</json:string><json:string>biopolymers pept</json:string><json:string>azasn carboxamide</json:string><json:string>intramolecular hydrogen bond</json:string><json:string>perkin trans</json:string></teeft></keywords><author><json:item><name>FRÉDÉRIC ANDRÉ</name><affiliations><json:string>LCPM, CNRS‐URA‐494, ENSIC‐INPL, Nancy, France, and</json:string></affiliations></json:item><json:item><name>ANDRÉ VICHERAT</name><affiliations><json:string>LCPM, CNRS‐URA‐494, ENSIC‐INPL, Nancy, France, and</json:string></affiliations></json:item><json:item><name>GUY BOUSSARD</name><affiliations><json:string>LCPM, CNRS‐URA‐494, ENSIC‐INPL, Nancy, France, and</json:string><json:string>Address: Dr. G. Boussard LCPM, ENSIC‐INPL BP451, 1 rue Grandville 54001 Nancy Cedex France Phone:+33 383 1751 96 Fax: +33 383 37 99 77 E‐mail: boussard@lcpm.ensic.u‐nancy.fr</json:string></affiliations></json:item><json:item><name>ANDRÉ AUBRY</name><affiliations><json:string>LCM3B, CNRS‐URA‐809, University Henri Poincaré, Vandazuvre, France</json:string></affiliations></json:item><json:item><name>MICHEL MARRAUD</name><affiliations><json:string>LCPM, CNRS‐URA‐494, ENSIC‐INPL, Nancy, France, and</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>aza‐alanine; aza‐asparagine</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>aza‐aspartic acid</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>β‐tum</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>IR study</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>pseudopeptide</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>structural analysis</value></json:item></subject><articleId><json:string>CBDD372</json:string></articleId><language><json:string>eng</json:string></language><originalGenre><json:string>article</json:string></originalGenre><abstract>To determine the structural perturbations induced by the CαH→Nα exchange in aza‐peptides, we have examined by H NMR and IR spectroscopy various derivatives of the aza‐analogues of alanine, aspartic acid and asparagine in different organic solvents with increasing polarity. Their general formulas are: R'‐AzXaa‐NR2R3, R'‐Pro‐AzXaa‐NR2R3 and R‐AzXaa‐Pro‐NR2R3 (where AzXaa denotes the aza‐analogue of the amino acid residue Xaa = Ala, Asp, Asn; R = Boc, Z; R2, R3= H, Me, iPr). The aza‐analogue of an amino acid residue appears to be a strong p‐turn‐inducing motif, and the AzAsn carboxamide side‐chain is capable of interacting, as a proton donor, with the preceding peptide carbonyl group.</abstract><qualityIndicators><score>6.072</score><pdfVersion>1.4</pdfVersion><pdfPageSize>612 x 792 pts (letter)</pdfPageSize><refBibsNative>true</refBibsNative><abstractCharCount>690</abstractCharCount><pdfWordCount>4324</pdfWordCount><pdfCharCount>27732</pdfCharCount><pdfPageCount>10</pdfPageCount><abstractWordCount>104</abstractWordCount></qualityIndicators><title>Aza‐peptides. III. Experimental structural analysis of aza‐alanme and aza‐asparagine‐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>5</issue><pages><first>372</first><last>381</last><total>10</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.tb01197.x</json:string></doi><id>61BD6B420D447C2DBB69BCCF8819B7965C87087A</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/document/61BD6B420D447C2DBB69BCCF8819B7965C87087A/fulltext/pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/document/61BD6B420D447C2DBB69BCCF8819B7965C87087A/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/61BD6B420D447C2DBB69BCCF8819B7965C87087A/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main">Aza‐peptides. III. Experimental structural analysis of aza‐alanme and aza‐asparagine‐containing peptides</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>Blackwell Publishing Ltd</publisher><pubPlace>Oxford, UK</pubPlace><date type="published" when="1997-11"></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">Aza‐peptides. III. Experimental structural analysis of aza‐alanme and aza‐asparagine‐containing peptides</title><author xml:id="author-0000"><persName><forename type="first">FRÉDÉRIC</forename><surname>ANDRÉ</surname></persName><affiliation>LCPM, CNRS‐URA‐494, ENSIC‐INPL, Nancy, France, and<address><country key="FR"></country></address></affiliation></author><author xml:id="author-0001"><persName><forename type="first">ANDRÉ</forename><surname>VICHERAT</surname></persName><affiliation>LCPM, CNRS‐URA‐494, ENSIC‐INPL, Nancy, France, and<address><country key="FR"></country></address></affiliation></author><author xml:id="author-0002" role="corresp"><persName><forename type="first">GUY</forename><surname>BOUSSARD</surname></persName><affiliation>LCPM, CNRS‐URA‐494, ENSIC‐INPL, Nancy, France, and<address><country key="FR"></country></address></affiliation><affiliation>Address: Dr. G. Boussard LCPM, ENSIC‐INPL BP451, 1 rue Grandville 54001 Nancy Cedex France Phone:+33 383 1751 96 Fax: +33 383 37 99 77 E‐mail: boussard@lcpm.ensic.u‐nancy.fr</affiliation></author><author xml:id="author-0003"><persName><forename type="first">ANDRÉ</forename><surname>AUBRY</surname></persName><affiliation>LCM3B, CNRS‐URA‐809, University Henri Poincaré, Vandazuvre, France<address><country key="FR"></country></address></affiliation></author><author xml:id="author-0004"><persName><forename type="first">MICHEL</forename><surname>MARRAUD</surname></persName><affiliation>LCPM, CNRS‐URA‐494, ENSIC‐INPL, Nancy, France, and<address><country key="FR"></country></address></affiliation></author><idno type="istex">61BD6B420D447C2DBB69BCCF8819B7965C87087A</idno><idno type="ark">ark:/67375/WNG-NZCV17SN-0</idno><idno type="DOI">10.1111/j.1399-3011.1997.tb01197.x</idno><idno type="unit">CBDD372</idno><idno type="toTypesetVersion">file:CBDD.CBDD372.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-5</idno><idno type="product">CBDD</idno><idno type="publisherDivision">ST</idno><imprint><biblScope unit="vol">50</biblScope><biblScope unit="issue">5</biblScope><biblScope unit="page" from="372">372</biblScope><biblScope unit="page" to="381">381</biblScope><biblScope unit="page-count">10</biblScope><publisher>Blackwell Publishing Ltd</publisher><pubPlace>Oxford, UK</pubPlace><date type="published" when="1997-11"></date></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><abstract xml:lang="en" style="main"><p>To determine the structural perturbations induced by the CαH→Nα exchange in aza‐peptides, we have examined by H NMR and IR spectroscopy various derivatives of the aza‐analogues of alanine, aspartic acid and asparagine in different organic solvents with increasing polarity. Their general formulas are: R'‐AzXaa‐NR<hi rend="superscript">2</hi>R<hi rend="superscript">3</hi>, R'‐Pro‐AzXaa‐NR<hi rend="superscript">2</hi>R<hi rend="superscript">3</hi> and R‐AzXaa‐Pro‐NR<hi rend="superscript">2</hi>R<hi rend="superscript">3</hi> (where AzXaa denotes the aza‐analogue of the amino acid residue Xaa = Ala, Asp, Asn; R = Boc, Z; R<hi rend="superscript">2</hi>, R<hi rend="superscript">3</hi>= H, Me, iPr). The aza‐analogue of an amino acid residue appears to be a strong p‐turn‐inducing motif, and the AzAsn carboxamide side‐chain is capable of interacting, as a proton donor, with the preceding peptide carbonyl group.</p></abstract><textClass><keywords xml:lang="en"><term xml:id="k1">aza‐alanine; aza‐asparagine</term><term xml:id="k2">aza‐aspartic acid</term><term xml:id="k3">aza‐peptides</term><term xml:id="k4">β‐tum</term><term xml:id="k5">IR study</term><term xml:id="k6">pseudopeptide</term><term xml:id="k7">structural analysis</term></keywords><keywords rend="tocHeading1"><term>Article</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/61BD6B420D447C2DBB69BCCF8819B7965C87087A/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)1399-3011</doi><issn type="print">1397-002X</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="JOURNAL OF PEPTIDE RESEARCH">The Journal of Peptide Research</title></titleGroup></publicationMeta><publicationMeta level="part" position="11005"><doi origin="wiley">10.1111/jpp.1997.50.issue-5</doi><numberingGroup><numbering type="journalVolume" number="50">50</numbering><numbering type="journalIssue" number="5">5</numbering></numberingGroup><coverDate startDate="1997-11">November 1997</coverDate></publicationMeta><publicationMeta level="unit" type="article" position="0037200" status="forIssue"><doi origin="wiley">10.1111/j.1399-3011.1997.tb01197.x</doi><idGroup><id type="unit" value="CBDD372"></id></idGroup><countGroup><count type="pageTotal" number="10"></count></countGroup><titleGroup><title type="tocHeading1">Article</title></titleGroup><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:2.3.2 mode:FullText source:HeaderRef result:HeaderRef" date="2010-03-04"></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="2014-11-04"></event></eventGroup><numberingGroup><numbering type="pageFirst" number="372">372</numbering><numbering type="pageLast" number="381">381</numbering></numberingGroup><correspondenceTo>Address: Dr. G. Boussard LCPM, ENSIC‐INPL BP451, 1 rue Grandville 54001 Nancy Cedex France Phone:+33 383 1751 96 Fax: +33 383 37 99 77 E‐mail: boussard@lcpm.ensic.u‐nancy.fr</correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:CBDD.CBDD372.pdf"></link></linkGroup></publicationMeta><contentMeta><unparsedEditorialHistory>Received 21 February, revised 18 April, accepted for publication 28 June 1997</unparsedEditorialHistory><countGroup><count type="referenceTotal" number="28"></count><count type="linksCrossRef" number="6"></count></countGroup><titleGroup><title type="main">Aza‐peptides. III. Experimental structural analysis of aza‐alanme and aza‐asparagine‐containing peptides</title></titleGroup><creators><creator creatorRole="author" xml:id="cr1" affiliationRef="#a1"><personName><givenNames>FRÉDÉRIC</givenNames><familyName>ANDRÉ</familyName></personName></creator><creator creatorRole="author" xml:id="cr2" affiliationRef="#a1"><personName><givenNames>ANDRÉ</givenNames><familyName>VICHERAT</familyName></personName></creator><creator creatorRole="author" xml:id="cr3" affiliationRef="#a1" corresponding="yes"><personName><givenNames>GUY</givenNames><familyName>BOUSSARD</familyName></personName></creator><creator creatorRole="author" xml:id="cr4" affiliationRef="#a2"><personName><givenNames>ANDRÉ</givenNames><familyName>AUBRY</familyName></personName></creator><creator creatorRole="author" xml:id="cr5" affiliationRef="#a1"><personName><givenNames>MICHEL</givenNames><familyName>MARRAUD</familyName></personName></creator></creators><affiliationGroup><affiliation xml:id="a1" countryCode="FR"><unparsedAffiliation>LCPM, CNRS‐URA‐494, ENSIC‐INPL, Nancy, France, and</unparsedAffiliation></affiliation><affiliation xml:id="a2" countryCode="FR"><unparsedAffiliation>LCM3B, CNRS‐URA‐809, University Henri Poincaré, Vandazuvre, France</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en"><keyword xml:id="k1">aza‐alanine; aza‐asparagine</keyword><keyword xml:id="k2">aza‐aspartic acid</keyword><keyword xml:id="k3">aza‐peptides</keyword><keyword xml:id="k4">β‐tum</keyword><keyword xml:id="k5">IR study</keyword><keyword xml:id="k6">pseudopeptide</keyword><keyword xml:id="k7">structural analysis</keyword></keywordGroup><abstractGroup><abstract type="main" xml:lang="en"><p>To determine the structural perturbations induced by the CαH→Nα exchange in aza‐peptides, we have examined by H NMR and IR spectroscopy various derivatives of the aza‐analogues of alanine, aspartic acid and asparagine in different organic solvents with increasing polarity. Their general formulas are: R'‐AzXaa‐NR<sup>2</sup>R<sup>3</sup>, R'‐Pro‐AzXaa‐NR<sup>2</sup>R<sup>3</sup> and R‐AzXaa‐Pro‐NR<sup>2</sup>R<sup>3</sup> (where AzXaa denotes the aza‐analogue of the amino acid residue Xaa = Ala, Asp, Asn; R = Boc, Z; R<sup>2</sup>, R<sup>3</sup>= H, Me, iPr). The aza‐analogue of an amino acid residue appears to be a strong p‐turn‐inducing motif, and the AzAsn carboxamide side‐chain is capable of interacting, as a proton donor, with the preceding peptide carbonyl group.</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Aza‐peptides. III. Experimental structural analysis of aza‐alanme and aza‐asparagine‐containing peptides</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Aza‐peptides. III. Experimental structural analysis of aza‐alanme and aza‐asparagine‐containing peptides</title></titleInfo><name type="personal"><namePart type="given">FRÉDÉRIC</namePart><namePart type="family">ANDRÉ</namePart><affiliation>LCPM, CNRS‐URA‐494, ENSIC‐INPL, Nancy, France, and</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">ANDRÉ</namePart><namePart type="family">VICHERAT</namePart><affiliation>LCPM, CNRS‐URA‐494, ENSIC‐INPL, Nancy, France, and</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, and</affiliation><affiliation>Correspondence address: Address: Dr. G. Boussard LCPM, ENSIC‐INPL BP451, 1 rue Grandville 54001 Nancy Cedex France Phone:+33 383 1751 96 Fax: +33 383 37 99 77 E‐mail: boussard@lcpm.ensic.u‐nancy.fr</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, Vandazuvre, 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, and</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">1997-11</dateIssued><edition>Received 21 February, revised 18 April, accepted for publication 28 June 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">28</extent><extent unit="linksCrossRef">6</extent></physicalDescription><abstract lang="en">To determine the structural perturbations induced by the CαH→Nα exchange in aza‐peptides, we have examined by H NMR and IR spectroscopy various derivatives of the aza‐analogues of alanine, aspartic acid and asparagine in different organic solvents with increasing polarity. Their general formulas are: R'‐AzXaa‐NR2R3, R'‐Pro‐AzXaa‐NR2R3 and R‐AzXaa‐Pro‐NR2R3 (where AzXaa denotes the aza‐analogue of the amino acid residue Xaa = Ala, Asp, Asn; R = Boc, Z; R2, R3= H, Me, iPr). The aza‐analogue of an amino acid residue appears to be a strong p‐turn‐inducing motif, and the AzAsn carboxamide side‐chain is capable of interacting, as a proton donor, with the preceding peptide carbonyl group.</abstract><subject lang="en"><genre>keywords</genre><topic>aza‐alanine; aza‐asparagine</topic><topic>aza‐aspartic acid</topic><topic>aza‐peptides</topic><topic>β‐tum</topic><topic>IR study</topic><topic>pseudopeptide</topic><topic>structural analysis</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>5</number></detail><extent unit="pages"><start>372</start><end>381</end><total>10</total></extent></part></relatedItem><identifier type="istex">61BD6B420D447C2DBB69BCCF8819B7965C87087A</identifier><identifier type="ark">ark:/67375/WNG-NZCV17SN-0</identifier><identifier type="DOI">10.1111/j.1399-3011.1997.tb01197.x</identifier><identifier type="ArticleID">CBDD372</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/61BD6B420D447C2DBB69BCCF8819B7965C87087A/metadata/json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Lorraine/explor/LrgpV1/Data/Istex/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000623 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Istex/Corpus/biblio.hfd -nk 000623 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Wicri/Lorraine
|area= LrgpV1
|flux= Istex
|étape= Corpus
|type= RBID
|clé= ISTEX:61BD6B420D447C2DBB69BCCF8819B7965C87087A
|texte= Aza‐peptides. III. Experimental structural analysis of aza‐alanme and aza‐asparagine‐containing peptides
}}
| This area was generated with Dilib version V0.6.32. |  |