AustralieFrV1, PascalFrancis, Curation, bibRecord, 004D16

Folding pentapeptides into left and right handed alpha helices

Identifieur interne : 004D16 ( PascalFrancis/Curation ); précédent : 004D15; suivant : 004D17

Folding pentapeptides into left and right handed alpha helices

Auteurs : Huy N. Hoang [Australie] ; Giovanni Abbenante [Australie] ; Timothy A. Hill [Australie] ; Gloria Ruiz-Gomez [Australie] ; David P. Fairlie [Australie]

Source :

Tetrahedron : (Oxford. Print) [ 0040-4020 ] ; 2012.

RBID : Pascal:12-0322341

Descripteurs français

Pascal (Inist)
- Pliage, Pentapeptide, Structure hélice, Hélicité, Composé chiral, Protéine, Alanine racemase, Spectrométrie CD, Structure moléculaire, Système tampon, Peptide cyclique, Eau, Conformation, Chiralité, Dichroïsme circulaire, Phosphate, Phosphore Composé organique, Foldamère.
Wicri :
- topic : Eau, Phosphate.

English descriptors

KwdEn :
- Alanine racemase, Buffer system, Chiral compound, Chirality, Circular dichroism, Circular dichroism spectrometry, Conformation, Cyclic peptides, Folding, Helical structure, Helicity, Molecular structure, Pentapeptide, Phosphates, Phosphorus Organic compounds, Protein, Water.

Abstract

Left or right handed alpha helicity can be induced in a pentapeptide (ANGYG) by appending left or right handed helical cycles as chiral templates. This sequence corresponds to a rare left handed helix found in the protein alanine racemase. Circular dichroism spectra reveal that pentapeptide ANGYG has no detectable structure in aq phosphate buffer, that it is an ambidextrous peptide in that it can be directed to fold into either a left handed or right handed alpha helix in water, with greater propensity for the uncommon left handed than the normal right handed conformation. A helix-inducing cyclic peptide at both ends of this peptide was more effective at inducing alpha helicity than a single cyclic peptide at one end. The alpha helical cyclic peptides provide novel tools for folding short peptides into thermodynamically unstable helices in water, and for studying factors that control chirality and helix induction.

A01	`01`	`1`		`@0 0040-4020`
A02	`01`			`@0 TETRAB`
A03		`1`		`@0 Tetrahedron : (Oxf. Print)`
A05				`@2 68`
A06				`@2 23`
A08	`01`	`1`	`ENG`	`@1 Folding pentapeptides into left and right handed alpha helices`
A09	`01`	`1`	`ENG`	`@1 Chemistry of Foldamers`
A11	`01`	`1`		`@1 HOANG (Huy N.)`
A11	`02`	`1`		`@1 ABBENANTE (Giovanni)`
A11	`03`	`1`		`@1 HILL (Timothy A.)`
A11	`04`	`1`		`@1 RUIZ-GOMEZ (Gloria)`
A11	`05`	`1`		`@1 FAIRLIE (David P.)`
A12	`01`	`1`		`@1 GUICHARD (Gilles) @9 ed.`
A12	`02`	`1`		`@1 HUC (Ivan) @9 ed.`
A14	`01`			`@1 Division of Chemistry and Structural Biology, Institute for Molecular Bioscience, The University of Queensland @2 Brisbane, Queensland 4072 @3 AUS @Z 1 aut. @Z 2 aut. @Z 3 aut. @Z 4 aut. @Z 5 aut.`
A15	`01`			`@1 Université de Bordeaux-CNRS UMR5248, Institut Européen de Chimie et Biologie @2 Pessac @3 FRA @Z 1 aut. @Z 2 aut.`
A20				`@2 4335, 4513-4516 [5 p.]`
A21				`@1 2012`
A23	`01`			`@0 ENG`
A43	`01`			`@1 INIST @2 8899 @5 354000506981670250`
A44				`@0 0000 @1 © 2012 INIST-CNRS. All rights reserved.`
A45				`@0 14 ref.`
A47	`01`	`1`		`@0 12-0322341`
A60				`@1 P`
A61				`@0 A`
A64	`01`	`1`		`@0 Tetrahedron : (Oxford. Print)`
A66	`01`			`@0 GBR`
C01	`01`		`ENG`	@0 Left or right handed alpha helicity can be induced in a pentapeptide (ANGYG) by appending left or right handed helical cycles as chiral templates. This sequence corresponds to a rare left handed helix found in the protein alanine racemase. Circular dichroism spectra reveal that pentapeptide ANGYG has no detectable structure in aq phosphate buffer, that it is an ambidextrous peptide in that it can be directed to fold into either a left handed or right handed alpha helix in water, with greater propensity for the uncommon left handed than the normal right handed conformation. A helix-inducing cyclic peptide at both ends of this peptide was more effective at inducing alpha helicity than a single cyclic peptide at one end. The alpha helical cyclic peptides provide novel tools for folding short peptides into thermodynamically unstable helices in water, and for studying factors that control chirality and helix induction.
C02	`01`	`X`		`@0 002A02D`
C02	`02`	`X`		`@0 001C03C08`
C02	`03`	`X`		`@0 001C03C01A`
C03	`01`	`X`	`FRE`	`@0 Pliage @5 01`
C03	`01`	`X`	`ENG`	`@0 Folding @5 01`
C03	`01`	`X`	`SPA`	`@0 Doblado @5 01`
C03	`02`	`X`	`FRE`	`@0 Pentapeptide @5 02`
C03	`02`	`X`	`ENG`	`@0 Pentapeptide @5 02`
C03	`02`	`X`	`SPA`	`@0 Pentapéptido @5 02`
C03	`03`	`X`	`FRE`	`@0 Structure hélice @5 03`
C03	`03`	`X`	`ENG`	`@0 Helical structure @5 03`
C03	`03`	`X`	`SPA`	`@0 Estructura helicoidal @5 03`
C03	`04`	`X`	`FRE`	`@0 Hélicité @5 04`
C03	`04`	`X`	`ENG`	`@0 Helicity @5 04`
C03	`04`	`X`	`SPA`	`@0 Helicidad @5 04`
C03	`05`	`X`	`FRE`	`@0 Composé chiral @5 05`
C03	`05`	`X`	`ENG`	`@0 Chiral compound @5 05`
C03	`05`	`X`	`SPA`	`@0 Compuesto quiral @5 05`
C03	`06`	`X`	`FRE`	`@0 Protéine @5 06`
C03	`06`	`X`	`ENG`	`@0 Protein @5 06`
C03	`06`	`X`	`SPA`	`@0 Proteína @5 06`
C03	`07`	`X`	`FRE`	`@0 Alanine racemase @2 FE @5 07`
C03	`07`	`X`	`ENG`	`@0 Alanine racemase @2 FE @5 07`
C03	`07`	`X`	`SPA`	`@0 Alanine racemase @2 FE @5 07`
C03	`08`	`X`	`FRE`	`@0 Spectrométrie CD @5 08`
C03	`08`	`X`	`ENG`	`@0 Circular dichroism spectrometry @5 08`
C03	`08`	`X`	`SPA`	`@0 Espectrometría CD @5 08`
C03	`09`	`X`	`FRE`	`@0 Structure moléculaire @5 09`
C03	`09`	`X`	`ENG`	`@0 Molecular structure @5 09`
C03	`09`	`X`	`SPA`	`@0 Estructura molecular @5 09`
C03	`10`	`X`	`FRE`	`@0 Système tampon @5 11`
C03	`10`	`X`	`ENG`	`@0 Buffer system @5 11`
C03	`10`	`X`	`SPA`	`@0 Sistema amortiguador @5 11`
C03	`11`	`X`	`FRE`	`@0 Peptide cyclique @5 12`
C03	`11`	`X`	`ENG`	`@0 Cyclic peptides @5 12`
C03	`11`	`X`	`SPA`	`@0 Péptido cíclico @5 12`
C03	`12`	`X`	`FRE`	`@0 Eau @5 13`
C03	`12`	`X`	`ENG`	`@0 Water @5 13`
C03	`12`	`X`	`SPA`	`@0 Agua @5 13`
C03	`13`	`X`	`FRE`	`@0 Conformation @5 14`
C03	`13`	`X`	`ENG`	`@0 Conformation @5 14`
C03	`13`	`X`	`SPA`	`@0 Conformación @5 14`
C03	`14`	`X`	`FRE`	`@0 Chiralité @5 15`
C03	`14`	`X`	`ENG`	`@0 Chirality @5 15`
C03	`14`	`X`	`SPA`	`@0 Quiralidad @5 15`
C03	`15`	`X`	`FRE`	`@0 Dichroïsme circulaire @5 16`
C03	`15`	`X`	`ENG`	`@0 Circular dichroism @5 16`
C03	`15`	`X`	`SPA`	`@0 Dicroismo circular @5 16`
C03	`16`	`X`	`FRE`	`@0 Phosphate @2 NA @5 17`
C03	`16`	`X`	`ENG`	`@0 Phosphates @2 NA @5 17`
C03	`16`	`X`	`SPA`	`@0 Fosfato @2 NA @5 17`
C03	`17`	`X`	`FRE`	`@0 Phosphore Composé organique @2 NC @2 NA @5 41`
C03	`17`	`X`	`ENG`	`@0 Phosphorus Organic compounds @2 NC @2 NA @5 41`
C03	`17`	`X`	`SPA`	`@0 Fósforo Compuesto orgánico @2 NC @2 NA @5 41`
C03	`18`	`X`	`FRE`	`@0 Foldamère @4 INC @5 62`
C07	`01`	`X`	`FRE`	`@0 Isomerases @2 FE`
C07	`01`	`X`	`ENG`	`@0 Isomerases @2 FE`
C07	`01`	`X`	`SPA`	`@0 Isomerases @2 FE`
C07	`02`	`X`	`FRE`	`@0 Enzyme @2 FE`
C07	`02`	`X`	`ENG`	`@0 Enzyme @2 FE`
C07	`02`	`X`	`SPA`	`@0 Enzima @2 FE`
N21				`@1 247`

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Pascal:12-0322341

Le document en format XML

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<author><name sortKey="Hoang, Huy N" sort="Hoang, Huy N" uniqKey="Hoang H" first="Huy N." last="Hoang">Huy N. Hoang</name>
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<author><name sortKey="Ruiz Gomez, Gloria" sort="Ruiz Gomez, Gloria" uniqKey="Ruiz Gomez G" first="Gloria" last="Ruiz-Gomez">Gloria Ruiz-Gomez</name>
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<s2>Brisbane, Queensland 4072</s2>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a">Folding pentapeptides into left and right handed alpha helices</title>
<author><name sortKey="Hoang, Huy N" sort="Hoang, Huy N" uniqKey="Hoang H" first="Huy N." last="Hoang">Huy N. Hoang</name>
<affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Division of Chemistry and Structural Biology, Institute for Molecular Bioscience, The University of Queensland</s1>
<s2>Brisbane, Queensland 4072</s2>
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<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
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<country>Australie</country>
</affiliation>
</author>
<author><name sortKey="Abbenante, Giovanni" sort="Abbenante, Giovanni" uniqKey="Abbenante G" first="Giovanni" last="Abbenante">Giovanni Abbenante</name>
<affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Division of Chemistry and Structural Biology, Institute for Molecular Bioscience, The University of Queensland</s1>
<s2>Brisbane, Queensland 4072</s2>
<s3>AUS</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
</inist:fA14>
<country>Australie</country>
</affiliation>
</author>
<author><name sortKey="Hill, Timothy A" sort="Hill, Timothy A" uniqKey="Hill T" first="Timothy A." last="Hill">Timothy A. Hill</name>
<affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Division of Chemistry and Structural Biology, Institute for Molecular Bioscience, The University of Queensland</s1>
<s2>Brisbane, Queensland 4072</s2>
<s3>AUS</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
</inist:fA14>
<country>Australie</country>
</affiliation>
</author>
<author><name sortKey="Ruiz Gomez, Gloria" sort="Ruiz Gomez, Gloria" uniqKey="Ruiz Gomez G" first="Gloria" last="Ruiz-Gomez">Gloria Ruiz-Gomez</name>
<affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Division of Chemistry and Structural Biology, Institute for Molecular Bioscience, The University of Queensland</s1>
<s2>Brisbane, Queensland 4072</s2>
<s3>AUS</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
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<country>Australie</country>
</affiliation>
</author>
<author><name sortKey="Fairlie, David P" sort="Fairlie, David P" uniqKey="Fairlie D" first="David P." last="Fairlie">David P. Fairlie</name>
<affiliation wicri:level="1"><inist:fA14 i1="01"><s1>Division of Chemistry and Structural Biology, Institute for Molecular Bioscience, The University of Queensland</s1>
<s2>Brisbane, Queensland 4072</s2>
<s3>AUS</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
</inist:fA14>
<country>Australie</country>
</affiliation>
</author>
</analytic>
<series><title level="j" type="main">Tetrahedron : (Oxford. Print)</title>
<title level="j" type="abbreviated">Tetrahedron : (Oxf. Print)</title>
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<title level="j" type="abbreviated">Tetrahedron : (Oxf. Print)</title>
<idno type="ISSN">0040-4020</idno>
</seriesStmt>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alanine racemase</term>
<term>Buffer system</term>
<term>Chiral compound</term>
<term>Chirality</term>
<term>Circular dichroism</term>
<term>Circular dichroism spectrometry</term>
<term>Conformation</term>
<term>Cyclic peptides</term>
<term>Folding</term>
<term>Helical structure</term>
<term>Helicity</term>
<term>Molecular structure</term>
<term>Pentapeptide</term>
<term>Phosphates</term>
<term>Phosphorus Organic compounds</term>
<term>Protein</term>
<term>Water</term>
</keywords>
<keywords scheme="Pascal" xml:lang="fr"><term>Pliage</term>
<term>Pentapeptide</term>
<term>Structure hélice</term>
<term>Hélicité</term>
<term>Composé chiral</term>
<term>Protéine</term>
<term>Alanine racemase</term>
<term>Spectrométrie CD</term>
<term>Structure moléculaire</term>
<term>Système tampon</term>
<term>Peptide cyclique</term>
<term>Eau</term>
<term>Conformation</term>
<term>Chiralité</term>
<term>Dichroïsme circulaire</term>
<term>Phosphate</term>
<term>Phosphore Composé organique</term>
<term>Foldamère</term>
</keywords>
<keywords scheme="Wicri" type="topic" xml:lang="fr"><term>Eau</term>
<term>Phosphate</term>
</keywords>
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<front><div type="abstract" xml:lang="en">Left or right handed alpha helicity can be induced in a pentapeptide (ANGYG) by appending left or right handed helical cycles as chiral templates. This sequence corresponds to a rare left handed helix found in the protein alanine racemase. Circular dichroism spectra reveal that pentapeptide ANGYG has no detectable structure in aq phosphate buffer, that it is an ambidextrous peptide in that it can be directed to fold into either a left handed or right handed alpha helix in water, with greater propensity for the uncommon left handed than the normal right handed conformation. A helix-inducing cyclic peptide at both ends of this peptide was more effective at inducing alpha helicity than a single cyclic peptide at one end. The alpha helical cyclic peptides provide novel tools for folding short peptides into thermodynamically unstable helices in water, and for studying factors that control chirality and helix induction.</div>
</front>
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</fA02>
<fA03 i2="1"><s0>Tetrahedron : (Oxf. Print)</s0>
</fA03>
<fA05><s2>68</s2>
</fA05>
<fA06><s2>23</s2>
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<fA08 i1="01" i2="1" l="ENG"><s1>Folding pentapeptides into left and right handed alpha helices</s1>
</fA08>
<fA09 i1="01" i2="1" l="ENG"><s1>Chemistry of Foldamers</s1>
</fA09>
<fA11 i1="01" i2="1"><s1>HOANG (Huy N.)</s1>
</fA11>
<fA11 i1="02" i2="1"><s1>ABBENANTE (Giovanni)</s1>
</fA11>
<fA11 i1="03" i2="1"><s1>HILL (Timothy A.)</s1>
</fA11>
<fA11 i1="04" i2="1"><s1>RUIZ-GOMEZ (Gloria)</s1>
</fA11>
<fA11 i1="05" i2="1"><s1>FAIRLIE (David P.)</s1>
</fA11>
<fA12 i1="01" i2="1"><s1>GUICHARD (Gilles)</s1>
<s9>ed.</s9>
</fA12>
<fA12 i1="02" i2="1"><s1>HUC (Ivan)</s1>
<s9>ed.</s9>
</fA12>
<fA14 i1="01"><s1>Division of Chemistry and Structural Biology, Institute for Molecular Bioscience, The University of Queensland</s1>
<s2>Brisbane, Queensland 4072</s2>
<s3>AUS</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
</fA14>
<fA15 i1="01"><s1>Université de Bordeaux-CNRS UMR5248, Institut Européen de Chimie et Biologie</s1>
<s2>Pessac</s2>
<s3>FRA</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
</fA15>
<fA20><s2>4335, 4513-4516 [5 p.]</s2>
</fA20>
<fA21><s1>2012</s1>
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<fA23 i1="01"><s0>ENG</s0>
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</fA45>
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</fA47>
<fA60><s1>P</s1>
</fA60>
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</fA61>
<fA64 i1="01" i2="1"><s0>Tetrahedron : (Oxford. Print)</s0>
</fA64>
<fA66 i1="01"><s0>GBR</s0>
</fA66>
<fC01 i1="01" l="ENG"><s0>Left or right handed alpha helicity can be induced in a pentapeptide (ANGYG) by appending left or right handed helical cycles as chiral templates. This sequence corresponds to a rare left handed helix found in the protein alanine racemase. Circular dichroism spectra reveal that pentapeptide ANGYG has no detectable structure in aq phosphate buffer, that it is an ambidextrous peptide in that it can be directed to fold into either a left handed or right handed alpha helix in water, with greater propensity for the uncommon left handed than the normal right handed conformation. A helix-inducing cyclic peptide at both ends of this peptide was more effective at inducing alpha helicity than a single cyclic peptide at one end. The alpha helical cyclic peptides provide novel tools for folding short peptides into thermodynamically unstable helices in water, and for studying factors that control chirality and helix induction.</s0>
</fC01>
<fC02 i1="01" i2="X"><s0>002A02D</s0>
</fC02>
<fC02 i1="02" i2="X"><s0>001C03C08</s0>
</fC02>
<fC02 i1="03" i2="X"><s0>001C03C01A</s0>
</fC02>
<fC03 i1="01" i2="X" l="FRE"><s0>Pliage</s0>
<s5>01</s5>
</fC03>
<fC03 i1="01" i2="X" l="ENG"><s0>Folding</s0>
<s5>01</s5>
</fC03>
<fC03 i1="01" i2="X" l="SPA"><s0>Doblado</s0>
<s5>01</s5>
</fC03>
<fC03 i1="02" i2="X" l="FRE"><s0>Pentapeptide</s0>
<s5>02</s5>
</fC03>
<fC03 i1="02" i2="X" l="ENG"><s0>Pentapeptide</s0>
<s5>02</s5>
</fC03>
<fC03 i1="02" i2="X" l="SPA"><s0>Pentapéptido</s0>
<s5>02</s5>
</fC03>
<fC03 i1="03" i2="X" l="FRE"><s0>Structure hélice</s0>
<s5>03</s5>
</fC03>
<fC03 i1="03" i2="X" l="ENG"><s0>Helical structure</s0>
<s5>03</s5>
</fC03>
<fC03 i1="03" i2="X" l="SPA"><s0>Estructura helicoidal</s0>
<s5>03</s5>
</fC03>
<fC03 i1="04" i2="X" l="FRE"><s0>Hélicité</s0>
<s5>04</s5>
</fC03>
<fC03 i1="04" i2="X" l="ENG"><s0>Helicity</s0>
<s5>04</s5>
</fC03>
<fC03 i1="04" i2="X" l="SPA"><s0>Helicidad</s0>
<s5>04</s5>
</fC03>
<fC03 i1="05" i2="X" l="FRE"><s0>Composé chiral</s0>
<s5>05</s5>
</fC03>
<fC03 i1="05" i2="X" l="ENG"><s0>Chiral compound</s0>
<s5>05</s5>
</fC03>
<fC03 i1="05" i2="X" l="SPA"><s0>Compuesto quiral</s0>
<s5>05</s5>
</fC03>
<fC03 i1="06" i2="X" l="FRE"><s0>Protéine</s0>
<s5>06</s5>
</fC03>
<fC03 i1="06" i2="X" l="ENG"><s0>Protein</s0>
<s5>06</s5>
</fC03>
<fC03 i1="06" i2="X" l="SPA"><s0>Proteína</s0>
<s5>06</s5>
</fC03>
<fC03 i1="07" i2="X" l="FRE"><s0>Alanine racemase</s0>
<s2>FE</s2>
<s5>07</s5>
</fC03>
<fC03 i1="07" i2="X" l="ENG"><s0>Alanine racemase</s0>
<s2>FE</s2>
<s5>07</s5>
</fC03>
<fC03 i1="07" i2="X" l="SPA"><s0>Alanine racemase</s0>
<s2>FE</s2>
<s5>07</s5>
</fC03>
<fC03 i1="08" i2="X" l="FRE"><s0>Spectrométrie CD</s0>
<s5>08</s5>
</fC03>
<fC03 i1="08" i2="X" l="ENG"><s0>Circular dichroism spectrometry</s0>
<s5>08</s5>
</fC03>
<fC03 i1="08" i2="X" l="SPA"><s0>Espectrometría CD</s0>
<s5>08</s5>
</fC03>
<fC03 i1="09" i2="X" l="FRE"><s0>Structure moléculaire</s0>
<s5>09</s5>
</fC03>
<fC03 i1="09" i2="X" l="ENG"><s0>Molecular structure</s0>
<s5>09</s5>
</fC03>
<fC03 i1="09" i2="X" l="SPA"><s0>Estructura molecular</s0>
<s5>09</s5>
</fC03>
<fC03 i1="10" i2="X" l="FRE"><s0>Système tampon</s0>
<s5>11</s5>
</fC03>
<fC03 i1="10" i2="X" l="ENG"><s0>Buffer system</s0>
<s5>11</s5>
</fC03>
<fC03 i1="10" i2="X" l="SPA"><s0>Sistema amortiguador</s0>
<s5>11</s5>
</fC03>
<fC03 i1="11" i2="X" l="FRE"><s0>Peptide cyclique</s0>
<s5>12</s5>
</fC03>
<fC03 i1="11" i2="X" l="ENG"><s0>Cyclic peptides</s0>
<s5>12</s5>
</fC03>
<fC03 i1="11" i2="X" l="SPA"><s0>Péptido cíclico</s0>
<s5>12</s5>
</fC03>
<fC03 i1="12" i2="X" l="FRE"><s0>Eau</s0>
<s5>13</s5>
</fC03>
<fC03 i1="12" i2="X" l="ENG"><s0>Water</s0>
<s5>13</s5>
</fC03>
<fC03 i1="12" i2="X" l="SPA"><s0>Agua</s0>
<s5>13</s5>
</fC03>
<fC03 i1="13" i2="X" l="FRE"><s0>Conformation</s0>
<s5>14</s5>
</fC03>
<fC03 i1="13" i2="X" l="ENG"><s0>Conformation</s0>
<s5>14</s5>
</fC03>
<fC03 i1="13" i2="X" l="SPA"><s0>Conformación</s0>
<s5>14</s5>
</fC03>
<fC03 i1="14" i2="X" l="FRE"><s0>Chiralité</s0>
<s5>15</s5>
</fC03>
<fC03 i1="14" i2="X" l="ENG"><s0>Chirality</s0>
<s5>15</s5>
</fC03>
<fC03 i1="14" i2="X" l="SPA"><s0>Quiralidad</s0>
<s5>15</s5>
</fC03>
<fC03 i1="15" i2="X" l="FRE"><s0>Dichroïsme circulaire</s0>
<s5>16</s5>
</fC03>
<fC03 i1="15" i2="X" l="ENG"><s0>Circular dichroism</s0>
<s5>16</s5>
</fC03>
<fC03 i1="15" i2="X" l="SPA"><s0>Dicroismo circular</s0>
<s5>16</s5>
</fC03>
<fC03 i1="16" i2="X" l="FRE"><s0>Phosphate</s0>
<s2>NA</s2>
<s5>17</s5>
</fC03>
<fC03 i1="16" i2="X" l="ENG"><s0>Phosphates</s0>
<s2>NA</s2>
<s5>17</s5>
</fC03>
<fC03 i1="16" i2="X" l="SPA"><s0>Fosfato</s0>
<s2>NA</s2>
<s5>17</s5>
</fC03>
<fC03 i1="17" i2="X" l="FRE"><s0>Phosphore Composé organique</s0>
<s2>NC</s2>
<s2>NA</s2>
<s5>41</s5>
</fC03>
<fC03 i1="17" i2="X" l="ENG"><s0>Phosphorus Organic compounds</s0>
<s2>NC</s2>
<s2>NA</s2>
<s5>41</s5>
</fC03>
<fC03 i1="17" i2="X" l="SPA"><s0>Fósforo Compuesto orgánico</s0>
<s2>NC</s2>
<s2>NA</s2>
<s5>41</s5>
</fC03>
<fC03 i1="18" i2="X" l="FRE"><s0>Foldamère</s0>
<s4>INC</s4>
<s5>62</s5>
</fC03>
<fC07 i1="01" i2="X" l="FRE"><s0>Isomerases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="01" i2="X" l="ENG"><s0>Isomerases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="01" i2="X" l="SPA"><s0>Isomerases</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="02" i2="X" l="FRE"><s0>Enzyme</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="02" i2="X" l="ENG"><s0>Enzyme</s0>
<s2>FE</s2>
</fC07>
<fC07 i1="02" i2="X" l="SPA"><s0>Enzima</s0>
<s2>FE</s2>
</fC07>
<fN21><s1>247</s1>
</fN21>
</pA>
</standard>
</inist>
</record>

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   |texte=   Folding pentapeptides into left and right handed alpha helices
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This area was generated with Dilib version V0.6.33.
Data generation: Tue Dec 5 10:43:12 2017. Site generation: Tue Mar 5 14:07:20 2024

	Serveur d'exploration sur les relations entre la France et l'Australie
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Serveur d'exploration sur les relations entre la France et l'Australie

Folding pentapeptides into left and right handed alpha helices

Folding pentapeptides into left and right handed alpha helices

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