Study of the hydrophobic cavity of beta-cryptogein through laser-polarized xenon NMR spectroscopy.
Identifieur interne : 001F67 ( Main/Exploration ); précédent : 001F66; suivant : 001F68Study of the hydrophobic cavity of beta-cryptogein through laser-polarized xenon NMR spectroscopy.
Auteurs : Patrick Berthault [France] ; Gaspard Huber ; Phuong Thu Ha ; Lionel Dubois ; Hervé Desvaux ; Eric GuittetSource :
- Chembiochem : a European journal of chemical biology [ 1439-4227 ] ; 2006.
Descripteurs français
- KwdFr :
- Conformation des protéines (MeSH), Cristallographie aux rayons X (MeSH), Interactions hydrophobes et hydrophiles (MeSH), Isotopes du carbone (MeSH), Lasers (MeSH), Modèles moléculaires (MeSH), Normes de référence (MeSH), Protons (MeSH), Protéines d'algue (composition chimique), Protéines fongiques (MeSH), Sensibilité et spécificité (MeSH), Sites de fixation (MeSH), Spectroscopie par résonance magnétique (méthodes), Spectroscopie par résonance magnétique (normes), Xénon (composition chimique), Xénon (effets des radiations).
- MESH :
- composition chimique : Protéines d'algue, Xénon.
- effets des radiations : Xénon.
- méthodes : Spectroscopie par résonance magnétique.
- normes : Spectroscopie par résonance magnétique.
- Conformation des protéines, Cristallographie aux rayons X, Interactions hydrophobes et hydrophiles, Isotopes du carbone, Lasers, Modèles moléculaires, Normes de référence, Protons, Protéines fongiques, Sensibilité et spécificité, Sites de fixation.
English descriptors
- KwdEn :
- Algal Proteins (chemistry), Binding Sites (MeSH), Carbon Isotopes (MeSH), Crystallography, X-Ray (MeSH), Fungal Proteins (MeSH), Hydrophobic and Hydrophilic Interactions (MeSH), Lasers (MeSH), Magnetic Resonance Spectroscopy (methods), Magnetic Resonance Spectroscopy (standards), Models, Molecular (MeSH), Protein Conformation (MeSH), Protons (MeSH), Reference Standards (MeSH), Sensitivity and Specificity (MeSH), Xenon (chemistry), Xenon (radiation effects).
- MESH :
- chemical , chemistry : Algal Proteins, Xenon.
- methods : Magnetic Resonance Spectroscopy.
- chemical , radiation effects : Xenon.
- standards : Magnetic Resonance Spectroscopy.
- Binding Sites, Carbon Isotopes, Crystallography, X-Ray, Fungal Proteins, Hydrophobic and Hydrophilic Interactions, Lasers, Models, Molecular, Protein Conformation, Protons, Reference Standards, Sensitivity and Specificity.
Abstract
The interaction of xenon with beta-cryptogein, a basic 10 kDa protein belonging to the elicitin family, has been studied by using dissolved thermal and laser-polarized gas in liquid-state NMR. 13C and 1H chemical-shift-mapping experiments were unfruitful, the proton lines only experienced a slight narrowing but no significant frequency variation when the xenon concentration was increased. Nevertheless magnetization transfer from hyperpolarized xenon to protons of the protein demonstrates an undoubted interaction and enables localization of the noble-gas-binding site. Due to the proton-proton cross-relaxation efficiency, however, this experiment is subjected to important spin-diffusion. An automatic procedure that takes spin-diffusion into account when assigning the protons that interact with xenon is then used. The binding site, as defined by 30 Xe--H interactions, is situated in the inner core of the protein. The protons that interact with xenon border the channel by which sterols are known to enter into the cavity. These results support the idea that xenon is a good probe for hydrophobic protein regions.
DOI: 10.1002/cbic.200500140
PubMed: 16292784
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Nevertheless magnetization transfer from hyperpolarized xenon to protons of the protein demonstrates an undoubted interaction and enables localization of the noble-gas-binding site. Due to the proton-proton cross-relaxation efficiency, however, this experiment is subjected to important spin-diffusion. An automatic procedure that takes spin-diffusion into account when assigning the protons that interact with xenon is then used. The binding site, as defined by 30 Xe--H interactions, is situated in the inner core of the protein. The protons that interact with xenon border the channel by which sterols are known to enter into the cavity. These results support the idea that xenon is a good probe for hydrophobic protein regions.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16292784</PMID><DateCompleted><Year>2006</Year><Month>04</Month><Day>06</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1439-4227</ISSN><JournalIssue CitedMedium="Print"><Volume>7</Volume><Issue>1</Issue><PubDate><Year>2006</Year><Month>Jan</Month></PubDate></JournalIssue><Title>Chembiochem : a European journal of chemical biology</Title><ISOAbbreviation>Chembiochem</ISOAbbreviation></Journal><ArticleTitle>Study of the hydrophobic cavity of beta-cryptogein through laser-polarized xenon NMR spectroscopy.</ArticleTitle><Pagination><MedlinePgn>59-64</MedlinePgn></Pagination><Abstract><AbstractText>The interaction of xenon with beta-cryptogein, a basic 10 kDa protein belonging to the elicitin family, has been studied by using dissolved thermal and laser-polarized gas in liquid-state NMR. 13C and 1H chemical-shift-mapping experiments were unfruitful, the proton lines only experienced a slight narrowing but no significant frequency variation when the xenon concentration was increased. Nevertheless magnetization transfer from hyperpolarized xenon to protons of the protein demonstrates an undoubted interaction and enables localization of the noble-gas-binding site. Due to the proton-proton cross-relaxation efficiency, however, this experiment is subjected to important spin-diffusion. An automatic procedure that takes spin-diffusion into account when assigning the protons that interact with xenon is then used. The binding site, as defined by 30 Xe--H interactions, is situated in the inner core of the protein. The protons that interact with xenon border the channel by which sterols are known to enter into the cavity. These results support the idea that xenon is a good probe for hydrophobic protein regions.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Berthault</LastName><ForeName>Patrick</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Laboratoire Structure et Dynamique par Résonance Magnétique, DSM/DRECAM/Service de Chimie Moléculaire, URA CEA/CNRS 331, CEA/Saclay, 91191 Gif sur Yvette, France. pberthault@cea.fr</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Huber</LastName><ForeName>Gaspard</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Ha</LastName><ForeName>Phuong Thu</ForeName><Initials>PT</Initials></Author><Author ValidYN="Y"><LastName>Dubois</LastName><ForeName>Lionel</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Desvaux</LastName><ForeName>Hervé</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Guittet</LastName><ForeName>Eric</ForeName><Initials>E</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Chembiochem</MedlineTA><NlmUniqueID>100937360</NlmUniqueID><ISSNLinking>1439-4227</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D020418">Algal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002247">Carbon Isotopes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance 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MajorTopicYN="N">Sensitivity and Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014978" MajorTopicYN="N">Xenon</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000528" MajorTopicYN="N">radiation effects</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2005</Year><Month>11</Month><Day>18</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2006</Year><Month>4</Month><Day>7</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2005</Year><Month>11</Month><Day>18</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">16292784</ArticleId><ArticleId IdType="doi">10.1002/cbic.200500140</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li></country><region><li>Île-de-France</li></region><settlement><li>Gif-sur-Yvette</li></settlement></list><tree><noCountry><name sortKey="Desvaux, Herve" sort="Desvaux, Herve" uniqKey="Desvaux H" first="Hervé" last="Desvaux">Hervé Desvaux</name><name sortKey="Dubois, Lionel" sort="Dubois, Lionel" uniqKey="Dubois L" first="Lionel" last="Dubois">Lionel Dubois</name><name sortKey="Guittet, Eric" sort="Guittet, Eric" uniqKey="Guittet E" first="Eric" last="Guittet">Eric Guittet</name><name sortKey="Ha, Phuong Thu" sort="Ha, Phuong Thu" uniqKey="Ha P" first="Phuong Thu" last="Ha">Phuong Thu Ha</name><name sortKey="Huber, Gaspard" sort="Huber, Gaspard" uniqKey="Huber G" first="Gaspard" last="Huber">Gaspard Huber</name></noCountry><country name="France"><region name="Île-de-France"><name sortKey="Berthault, Patrick" sort="Berthault, Patrick" uniqKey="Berthault P" 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