Study of amide proton exchange in 15N-enriched cryptogein using pH-dependent off-resonance ROESY-HSQC experiments.
Identifieur interne : 002962 ( Main/Exploration ); précédent : 002961; suivant : 002963Study of amide proton exchange in 15N-enriched cryptogein using pH-dependent off-resonance ROESY-HSQC experiments.
Auteurs : S. Fefeu [France] ; N. Birlirakis ; E. GuittetSource :
- European biophysics journal : EBJ [ 0175-7571 ] ; 1998.
Descripteurs français
- KwdFr :
- Amides (composition chimique), Concentration en ions d'hydrogène (MeSH), Conformation des protéines (MeSH), Eau (composition chimique), Isotopes de l'azote (MeSH), Modèles moléculaires (MeSH), Protons (MeSH), Protéines d'algue (MeSH), Protéines fongiques (composition chimique), Résonance magnétique nucléaire biomoléculaire (méthodes), Solvants (MeSH), Structure secondaire des protéines (MeSH).
- MESH :
English descriptors
- KwdEn :
- Algal Proteins (MeSH), Amides (chemistry), Fungal Proteins (chemistry), Hydrogen-Ion Concentration (MeSH), Models, Molecular (MeSH), Nitrogen Isotopes (MeSH), Nuclear Magnetic Resonance, Biomolecular (methods), Protein Conformation (MeSH), Protein Structure, Secondary (MeSH), Protons (MeSH), Solvents (MeSH), Water (chemistry).
- MESH :
- chemical , chemistry : Amides, Fungal Proteins, Water.
- chemical : Algal Proteins, Nitrogen Isotopes, Protons, Solvents.
- methods : Nuclear Magnetic Resonance, Biomolecular.
- Hydrogen-Ion Concentration, Models, Molecular, Protein Conformation, Protein Structure, Secondary.
Abstract
A new pH-dependent off-resonance ROESY-HSQC experiment has been used to characterize the degree of protection of the amide protons of cryptogein, a protein of the elicitin family, against solvent exchange. The study of the pH dependence of solvent-shielded amide protons in this protein reveals that the helices have different levels of stability. Two of the five helices exhibit strong protection of amide hydrogens against exchange with the solvent. By contrast, greater flexibility is observed in the other three helices, particularly in the C-terminal helix. These results provide information on the dynamic features of the protein and are consistent with the RMSD for the backbone atoms of residues involved in helical structures. In addition, the question of the flexibility in a hydrophobic cavity made of conserved residues, which represent a plausible binding site, is addressed by this method.
DOI: 10.1007/s002490050122
PubMed: 10950638
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Guittet</name></author></analytic><series><title level="j">European biophysics journal : EBJ</title><idno type="ISSN">0175-7571</idno><imprint><date when="1998" type="published">1998</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Algal Proteins (MeSH)</term><term>Amides (chemistry)</term><term>Fungal Proteins (chemistry)</term><term>Hydrogen-Ion Concentration (MeSH)</term><term>Models, Molecular (MeSH)</term><term>Nitrogen Isotopes (MeSH)</term><term>Nuclear Magnetic Resonance, Biomolecular (methods)</term><term>Protein Conformation (MeSH)</term><term>Protein Structure, Secondary (MeSH)</term><term>Protons (MeSH)</term><term>Solvents (MeSH)</term><term>Water (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Amides (composition chimique)</term><term>Concentration en ions d'hydrogène (MeSH)</term><term>Conformation des protéines (MeSH)</term><term>Eau (composition chimique)</term><term>Isotopes de l'azote (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>Protons (MeSH)</term><term>Protéines d'algue (MeSH)</term><term>Protéines fongiques (composition chimique)</term><term>Résonance magnétique nucléaire biomoléculaire (méthodes)</term><term>Solvants (MeSH)</term><term>Structure secondaire des protéines (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Amides</term><term>Fungal Proteins</term><term>Water</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Algal Proteins</term><term>Nitrogen Isotopes</term><term>Protons</term><term>Solvents</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Amides</term><term>Eau</term><term>Protéines fongiques</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Nuclear Magnetic Resonance, Biomolecular</term></keywords><keywords scheme="MESH" qualifier="méthodes" xml:lang="fr"><term>Résonance magnétique nucléaire biomoléculaire</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Hydrogen-Ion Concentration</term><term>Models, Molecular</term><term>Protein Conformation</term><term>Protein Structure, Secondary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Concentration en ions d'hydrogène</term><term>Conformation des protéines</term><term>Isotopes de l'azote</term><term>Modèles moléculaires</term><term>Protons</term><term>Protéines d'algue</term><term>Solvants</term><term>Structure secondaire des protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A new pH-dependent off-resonance ROESY-HSQC experiment has been used to characterize the degree of protection of the amide protons of cryptogein, a protein of the elicitin family, against solvent exchange. The study of the pH dependence of solvent-shielded amide protons in this protein reveals that the helices have different levels of stability. Two of the five helices exhibit strong protection of amide hydrogens against exchange with the solvent. By contrast, greater flexibility is observed in the other three helices, particularly in the C-terminal helix. These results provide information on the dynamic features of the protein and are consistent with the RMSD for the backbone atoms of residues involved in helical structures. In addition, the question of the flexibility in a hydrophobic cavity made of conserved residues, which represent a plausible binding site, is addressed by this method.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">10950638</PMID><DateCompleted><Year>2000</Year><Month>08</Month><Day>16</Day></DateCompleted><DateRevised><Year>2019</Year><Month>11</Month><Day>04</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0175-7571</ISSN><JournalIssue CitedMedium="Print"><Volume>27</Volume><Issue>2</Issue><PubDate><Year>1998</Year></PubDate></JournalIssue><Title>European biophysics journal : EBJ</Title><ISOAbbreviation>Eur Biophys J</ISOAbbreviation></Journal><ArticleTitle>Study of amide proton exchange in 15N-enriched cryptogein using pH-dependent off-resonance ROESY-HSQC experiments.</ArticleTitle><Pagination><MedlinePgn>167-71</MedlinePgn></Pagination><Abstract><AbstractText>A new pH-dependent off-resonance ROESY-HSQC experiment has been used to characterize the degree of protection of the amide protons of cryptogein, a protein of the elicitin family, against solvent exchange. The study of the pH dependence of solvent-shielded amide protons in this protein reveals that the helices have different levels of stability. Two of the five helices exhibit strong protection of amide hydrogens against exchange with the solvent. By contrast, greater flexibility is observed in the other three helices, particularly in the C-terminal helix. These results provide information on the dynamic features of the protein and are consistent with the RMSD for the backbone atoms of residues involved in helical structures. 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Birlirakis</name><name sortKey="Guittet, E" sort="Guittet, E" uniqKey="Guittet E" first="E" last="Guittet">E. Guittet</name></noCountry><country name="France"><region name="Île-de-France"><name sortKey="Fefeu, S" sort="Fefeu, S" uniqKey="Fefeu S" first="S" last="Fefeu">S. Fefeu</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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