Influence of drying on the secondary structure of intrinsically disordered and globular proteins.
Identifieur interne : 000225 ( Main/Exploration ); précédent : 000224; suivant : 000226Influence of drying on the secondary structure of intrinsically disordered and globular proteins.
Auteurs : Michaela Hundertmark [Allemagne] ; Antoaneta V. Popova ; Saskia Rausch ; Robert Seckler ; Dirk K. HinchaSource :
- Biochemical and biophysical research communications [ 1090-2104 ] ; 2012.
Descripteurs français
- KwdFr :
- Dessiccation (MeSH), Dichroïsme circulaire (MeSH), Données de séquences moléculaires (MeSH), Glucides (composition chimique), Lactoglobulines (composition chimique), Oligosaccharides (composition chimique), Pancreatic ribonuclease (composition chimique), Pliage des protéines (MeSH), Protéines d'Arabidopsis (composition chimique), Protéines végétales (composition chimique), Solubilité (MeSH), Solutions (MeSH), Spectroscopie infrarouge à transformée de Fourier (MeSH), Structure secondaire des protéines (MeSH), Séquence d'acides aminés (MeSH), Sérumalbumine bovine (composition chimique).
- MESH :
- composition chimique : Glucides, Lactoglobulines, Oligosaccharides, Pancreatic ribonuclease, Protéines d'Arabidopsis, Protéines végétales, Sérumalbumine bovine.
- Dessiccation, Dichroïsme circulaire, Données de séquences moléculaires, Pliage des protéines, Solubilité, Solutions, Spectroscopie infrarouge à transformée de Fourier, Structure secondaire des protéines, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Arabidopsis Proteins (chemistry), Carbohydrates (chemistry), Circular Dichroism (MeSH), Desiccation (MeSH), Lactoglobulins (chemistry), Molecular Sequence Data (MeSH), Oligosaccharides (chemistry), Plant Proteins (chemistry), Protein Folding (MeSH), Protein Structure, Secondary (MeSH), Ribonuclease, Pancreatic (chemistry), Serum Albumin, Bovine (chemistry), Solubility (MeSH), Solutions (MeSH), Spectroscopy, Fourier Transform Infrared (MeSH).
- MESH :
- chemical , chemistry : Arabidopsis Proteins, Carbohydrates, Lactoglobulins, Oligosaccharides, Plant Proteins, Ribonuclease, Pancreatic, Serum Albumin, Bovine.
- Amino Acid Sequence, Circular Dichroism, Desiccation, Molecular Sequence Data, Protein Folding, Protein Structure, Secondary, Solubility, Solutions, Spectroscopy, Fourier Transform Infrared.
Abstract
Circular dichroism (CD) spectroscopy of five Arabidopsis late embryogenesis abundant (LEA) proteins constituting the plant specific families LEA_5 and LEA_6 showed that they are intrinsically disordered in solution and partially fold during drying. Structural predictions were comparable to these results for hydrated LEA_6, but not for LEA_5 proteins. FTIR spectroscopy showed that verbascose, but not sucrose, strongly affected the structure of the dry proteins. The four investigated globular proteins were only mildly affected by drying in the absence, but strongly in the presence of sugars. These data highlight the larger structural flexibility of disordered compared to globular proteins and the impact of sugars on the structure of both disordered and globular proteins during drying.
DOI: 10.1016/j.bbrc.2011.11.067
PubMed: 22155233
Affiliations:
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Popova</name></author><author><name sortKey="Rausch, Saskia" sort="Rausch, Saskia" uniqKey="Rausch S" first="Saskia" last="Rausch">Saskia Rausch</name></author><author><name sortKey="Seckler, Robert" sort="Seckler, Robert" uniqKey="Seckler R" first="Robert" last="Seckler">Robert Seckler</name></author><author><name sortKey="Hincha, Dirk K" sort="Hincha, Dirk K" uniqKey="Hincha D" first="Dirk K" last="Hincha">Dirk K. Hincha</name></author></analytic><series><title level="j">Biochemical and biophysical research communications</title><idno type="eISSN">1090-2104</idno><imprint><date when="2012" type="published">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Arabidopsis Proteins (chemistry)</term><term>Carbohydrates (chemistry)</term><term>Circular Dichroism (MeSH)</term><term>Desiccation (MeSH)</term><term>Lactoglobulins (chemistry)</term><term>Molecular Sequence Data (MeSH)</term><term>Oligosaccharides (chemistry)</term><term>Plant Proteins (chemistry)</term><term>Protein Folding (MeSH)</term><term>Protein Structure, Secondary (MeSH)</term><term>Ribonuclease, Pancreatic (chemistry)</term><term>Serum Albumin, Bovine (chemistry)</term><term>Solubility (MeSH)</term><term>Solutions (MeSH)</term><term>Spectroscopy, Fourier Transform Infrared (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Dessiccation (MeSH)</term><term>Dichroïsme circulaire (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Glucides (composition chimique)</term><term>Lactoglobulines (composition chimique)</term><term>Oligosaccharides (composition chimique)</term><term>Pancreatic ribonuclease (composition chimique)</term><term>Pliage des protéines (MeSH)</term><term>Protéines d'Arabidopsis (composition chimique)</term><term>Protéines végétales (composition chimique)</term><term>Solubilité (MeSH)</term><term>Solutions (MeSH)</term><term>Spectroscopie infrarouge à transformée de Fourier (MeSH)</term><term>Structure secondaire des protéines (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Sérumalbumine bovine (composition chimique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Arabidopsis Proteins</term><term>Carbohydrates</term><term>Lactoglobulins</term><term>Oligosaccharides</term><term>Plant Proteins</term><term>Ribonuclease, Pancreatic</term><term>Serum Albumin, Bovine</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Glucides</term><term>Lactoglobulines</term><term>Oligosaccharides</term><term>Pancreatic ribonuclease</term><term>Protéines d'Arabidopsis</term><term>Protéines végétales</term><term>Sérumalbumine bovine</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Circular Dichroism</term><term>Desiccation</term><term>Molecular Sequence Data</term><term>Protein Folding</term><term>Protein Structure, Secondary</term><term>Solubility</term><term>Solutions</term><term>Spectroscopy, Fourier Transform Infrared</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Dessiccation</term><term>Dichroïsme circulaire</term><term>Données de séquences moléculaires</term><term>Pliage des protéines</term><term>Solubilité</term><term>Solutions</term><term>Spectroscopie infrarouge à transformée de Fourier</term><term>Structure secondaire des protéines</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Circular dichroism (CD) spectroscopy of five Arabidopsis late embryogenesis abundant (LEA) proteins constituting the plant specific families LEA_5 and LEA_6 showed that they are intrinsically disordered in solution and partially fold during drying. Structural predictions were comparable to these results for hydrated LEA_6, but not for LEA_5 proteins. FTIR spectroscopy showed that verbascose, but not sucrose, strongly affected the structure of the dry proteins. The four investigated globular proteins were only mildly affected by drying in the absence, but strongly in the presence of sugars. These data highlight the larger structural flexibility of disordered compared to globular proteins and the impact of sugars on the structure of both disordered and globular proteins during drying.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22155233</PMID><DateCompleted><Year>2012</Year><Month>03</Month><Day>22</Day></DateCompleted><DateRevised><Year>2017</Year><Month>11</Month><Day>16</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1090-2104</ISSN><JournalIssue CitedMedium="Internet"><Volume>417</Volume><Issue>1</Issue><PubDate><Year>2012</Year><Month>Jan</Month><Day>06</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem Biophys Res Commun</ISOAbbreviation></Journal><ArticleTitle>Influence of drying on the secondary structure of intrinsically disordered and globular proteins.</ArticleTitle><Pagination><MedlinePgn>122-8</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbrc.2011.11.067</ELocationID><Abstract><AbstractText>Circular dichroism (CD) spectroscopy of five Arabidopsis late embryogenesis abundant (LEA) proteins constituting the plant specific families LEA_5 and LEA_6 showed that they are intrinsically disordered in solution and partially fold during drying. Structural predictions were comparable to these results for hydrated LEA_6, but not for LEA_5 proteins. FTIR spectroscopy showed that verbascose, but not sucrose, strongly affected the structure of the dry proteins. The four investigated globular proteins were only mildly affected by drying in the absence, but strongly in the presence of sugars. These data highlight the larger structural flexibility of disordered compared to globular proteins and the impact of sugars on the structure of both disordered and globular proteins during drying.</AbstractText><CopyrightInformation>Copyright © 2011 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Hundertmark</LastName><ForeName>Michaela</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Max-Planck-Institut für Molekulare Pflanzenphysiologie, Potsdam, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Popova</LastName><ForeName>Antoaneta V</ForeName><Initials>AV</Initials></Author><Author ValidYN="Y"><LastName>Rausch</LastName><ForeName>Saskia</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Seckler</LastName><ForeName>Robert</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Hincha</LastName><ForeName>Dirk K</ForeName><Initials>DK</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><ArticleDate DateType="Electronic"><Year>2011</Year><Month>12</Month><Day>01</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochem Biophys Res Commun</MedlineTA><NlmUniqueID>0372516</NlmUniqueID><ISSNLinking>0006-291X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029681">Arabidopsis Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002241">Carbohydrates</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007782">Lactoglobulins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009844">Oligosaccharides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012996">Solutions</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C066246">late embryogenesis abundant protein, plant</NameOfSubstance></Chemical><Chemical><RegistryNumber>27432CM55Q</RegistryNumber><NameOfSubstance UI="D012710">Serum Albumin, Bovine</NameOfSubstance></Chemical><Chemical><RegistryNumber>53850-34-3</RegistryNumber><NameOfSubstance UI="C003427">thaumatin protein, plant</NameOfSubstance></Chemical><Chemical><RegistryNumber>75493766S3</RegistryNumber><NameOfSubstance UI="C570815">verbascose</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.27.5</RegistryNumber><NameOfSubstance UI="D012259">Ribonuclease, Pancreatic</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D029681" MajorTopicYN="N">Arabidopsis 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Transform Infrared</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2011</Year><Month>11</Month><Day>08</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2011</Year><Month>11</Month><Day>13</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2011</Year><Month>12</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2011</Year><Month>12</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2012</Year><Month>3</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">22155233</ArticleId><ArticleId IdType="pii">S0006-291X(11)02081-X</ArticleId><ArticleId IdType="doi">10.1016/j.bbrc.2011.11.067</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li></country><region><li>Brandebourg</li></region><settlement><li>Potsdam</li></settlement></list><tree><noCountry><name sortKey="Hincha, Dirk K" sort="Hincha, Dirk K" uniqKey="Hincha D" first="Dirk K" last="Hincha">Dirk K. Hincha</name><name sortKey="Popova, Antoaneta V" sort="Popova, Antoaneta V" uniqKey="Popova A" first="Antoaneta V" last="Popova">Antoaneta V. Popova</name><name sortKey="Rausch, Saskia" sort="Rausch, Saskia" uniqKey="Rausch S" first="Saskia" last="Rausch">Saskia Rausch</name><name sortKey="Seckler, Robert" sort="Seckler, Robert" uniqKey="Seckler R" first="Robert" last="Seckler">Robert Seckler</name></noCountry><country name="Allemagne"><region name="Brandebourg"><name sortKey="Hundertmark, Michaela" sort="Hundertmark, Michaela" uniqKey="Hundertmark M" first="Michaela" last="Hundertmark">Michaela Hundertmark</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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