Thermal stability of wild type and disulfide bridge containing mutant of poplar plastocyanin.
Identifieur interne : 004176 ( Main/Exploration ); précédent : 004175; suivant : 004177Thermal stability of wild type and disulfide bridge containing mutant of poplar plastocyanin.
Auteurs : Rita Guzzi [Italie] ; Laura Andolfi ; Salvatore Cannistraro ; Martin Ph Verbeet ; Gerard W. Canters ; Luigi SportelliSource :
- Biophysical chemistry [ 0301-4622 ] ; 2004.
Descripteurs français
- KwdFr :
- Calorimétrie différentielle à balayage (MeSH), Conformation des protéines (MeSH), Disulfures (composition chimique), Dénaturation des protéines (MeSH), Mutation (génétique), Plastocyanine (composition chimique), Plastocyanine (génétique), Pliage des protéines (MeSH), Populus (composition chimique), Spectrométrie de fluorescence (MeSH), Température élevée (MeSH), Thermodynamique (MeSH).
- MESH :
- composition chimique : Disulfures, Plastocyanine, Populus.
- génétique : Mutation, Plastocyanine.
- Calorimétrie différentielle à balayage, Conformation des protéines, Dénaturation des protéines, Pliage des protéines, Spectrométrie de fluorescence, Température élevée, Thermodynamique.
English descriptors
- KwdEn :
- Calorimetry, Differential Scanning (MeSH), Disulfides (chemistry), Hot Temperature (MeSH), Mutation (genetics), Plastocyanin (chemistry), Plastocyanin (genetics), Populus (chemistry), Protein Conformation (MeSH), Protein Denaturation (MeSH), Protein Folding (MeSH), Spectrometry, Fluorescence (MeSH), Thermodynamics (MeSH).
- MESH :
- chemical , chemistry : Disulfides, Plastocyanin.
- chemistry : Populus.
- genetics : Mutation, Plastocyanin.
- Calorimetry, Differential Scanning, Hot Temperature, Protein Conformation, Protein Denaturation, Protein Folding, Spectrometry, Fluorescence, Thermodynamics.
Abstract
A comparative study of the thermal stability of wild type poplar plastocyanin and of a mutant form containing a disulfide bridge between residues 21 and 25 was performed using differential scanning calorimetry and optical spectroscopic techniques. For wild type plastocyanin the transition temperature, determined from the calorimetric profiles, is 62.7 degrees C at the scan rate of 60 degrees C/h, whereas for the mutant it is reduced to 58.0 degrees C. In both cases, the endothermic peak is followed by an exothermic one at higher temperatures. The unfolding process monitored by optical absorption at 596 nm also reveals a reduced thermal stability of the mutated plastocyanin compared to the wild type protein, with transition temperatures of 54.8 and 58.0 degrees C, respectively. For both proteins, the denaturation process was found to be irreversible and dependent on the scan rate preventing the thermodynamic analysis of the unfolding process. In parallel, small conformational changes between wild type and mutant plastocyanin emerge from fluorescence spectroscopy measurements. Here, a difference in the interaction of the two proteins between the microenvironment surrounding the fluorophores and the solvent was proposed. The destabilization observed in the disulfide containing mutant of plastocyanin suggests that the double mutation, Ile21Cys and Glu25Cys, introduces strain into the protein which offsets the stabilizing effect expected from the formation of a covalent crosslink.
DOI: 10.1016/j.bpc.2004.07.002
PubMed: 15501574
Affiliations:
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Bucci, Cubo 31C, 87036 Rende</wicri:regionArea><wicri:noRegion>87036 Rende</wicri:noRegion></affiliation></author><author><name sortKey="Andolfi, Laura" sort="Andolfi, Laura" uniqKey="Andolfi L" first="Laura" last="Andolfi">Laura Andolfi</name></author><author><name sortKey="Cannistraro, Salvatore" sort="Cannistraro, Salvatore" uniqKey="Cannistraro S" first="Salvatore" last="Cannistraro">Salvatore Cannistraro</name></author><author><name sortKey="Verbeet, Martin Ph" sort="Verbeet, Martin Ph" uniqKey="Verbeet M" first="Martin Ph" last="Verbeet">Martin Ph Verbeet</name></author><author><name sortKey="Canters, Gerard W" sort="Canters, Gerard W" uniqKey="Canters G" first="Gerard W" last="Canters">Gerard W. Canters</name></author><author><name sortKey="Sportelli, Luigi" sort="Sportelli, Luigi" uniqKey="Sportelli L" first="Luigi" last="Sportelli">Luigi Sportelli</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2004">2004</date><idno type="RBID">pubmed:15501574</idno><idno type="pmid">15501574</idno><idno type="doi">10.1016/j.bpc.2004.07.002</idno><idno type="wicri:Area/Main/Corpus">004181</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">004181</idno><idno type="wicri:Area/Main/Curation">004181</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">004181</idno><idno type="wicri:Area/Main/Exploration">004181</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Thermal stability of wild type and disulfide bridge containing mutant of poplar plastocyanin.</title><author><name sortKey="Guzzi, Rita" sort="Guzzi, Rita" uniqKey="Guzzi R" first="Rita" last="Guzzi">Rita Guzzi</name><affiliation wicri:level="1"><nlm:affiliation>Dipartimento di Fisica and Unità INFM, Laboratorio di Biofisica Molecolare, Università della Calabria, Ponte P. Bucci, Cubo 31C, 87036 Rende, Italy. guzzi@fis.unical.it</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Dipartimento di Fisica and Unità INFM, Laboratorio di Biofisica Molecolare, Università della Calabria, Ponte P. Bucci, Cubo 31C, 87036 Rende</wicri:regionArea><wicri:noRegion>87036 Rende</wicri:noRegion></affiliation></author><author><name sortKey="Andolfi, Laura" sort="Andolfi, Laura" uniqKey="Andolfi L" first="Laura" last="Andolfi">Laura Andolfi</name></author><author><name sortKey="Cannistraro, Salvatore" sort="Cannistraro, Salvatore" uniqKey="Cannistraro S" first="Salvatore" last="Cannistraro">Salvatore Cannistraro</name></author><author><name sortKey="Verbeet, Martin Ph" sort="Verbeet, Martin Ph" uniqKey="Verbeet M" first="Martin Ph" last="Verbeet">Martin Ph Verbeet</name></author><author><name sortKey="Canters, Gerard W" sort="Canters, Gerard W" uniqKey="Canters G" first="Gerard W" last="Canters">Gerard W. Canters</name></author><author><name sortKey="Sportelli, Luigi" sort="Sportelli, Luigi" uniqKey="Sportelli L" first="Luigi" last="Sportelli">Luigi Sportelli</name></author></analytic><series><title level="j">Biophysical chemistry</title><idno type="ISSN">0301-4622</idno><imprint><date when="2004" type="published">2004</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Calorimetry, Differential Scanning (MeSH)</term><term>Disulfides (chemistry)</term><term>Hot Temperature (MeSH)</term><term>Mutation (genetics)</term><term>Plastocyanin (chemistry)</term><term>Plastocyanin (genetics)</term><term>Populus (chemistry)</term><term>Protein Conformation (MeSH)</term><term>Protein Denaturation (MeSH)</term><term>Protein Folding (MeSH)</term><term>Spectrometry, Fluorescence (MeSH)</term><term>Thermodynamics (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Calorimétrie différentielle à balayage (MeSH)</term><term>Conformation des protéines (MeSH)</term><term>Disulfures (composition chimique)</term><term>Dénaturation des protéines (MeSH)</term><term>Mutation (génétique)</term><term>Plastocyanine (composition chimique)</term><term>Plastocyanine (génétique)</term><term>Pliage des protéines (MeSH)</term><term>Populus (composition chimique)</term><term>Spectrométrie de fluorescence (MeSH)</term><term>Température élevée (MeSH)</term><term>Thermodynamique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Disulfides</term><term>Plastocyanin</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Disulfures</term><term>Plastocyanine</term><term>Populus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Mutation</term><term>Plastocyanin</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Mutation</term><term>Plastocyanine</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Calorimetry, Differential Scanning</term><term>Hot Temperature</term><term>Protein Conformation</term><term>Protein Denaturation</term><term>Protein Folding</term><term>Spectrometry, Fluorescence</term><term>Thermodynamics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Calorimétrie différentielle à balayage</term><term>Conformation des protéines</term><term>Dénaturation des protéines</term><term>Pliage des protéines</term><term>Spectrométrie de fluorescence</term><term>Température élevée</term><term>Thermodynamique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A comparative study of the thermal stability of wild type poplar plastocyanin and of a mutant form containing a disulfide bridge between residues 21 and 25 was performed using differential scanning calorimetry and optical spectroscopic techniques. For wild type plastocyanin the transition temperature, determined from the calorimetric profiles, is 62.7 degrees C at the scan rate of 60 degrees C/h, whereas for the mutant it is reduced to 58.0 degrees C. In both cases, the endothermic peak is followed by an exothermic one at higher temperatures. The unfolding process monitored by optical absorption at 596 nm also reveals a reduced thermal stability of the mutated plastocyanin compared to the wild type protein, with transition temperatures of 54.8 and 58.0 degrees C, respectively. For both proteins, the denaturation process was found to be irreversible and dependent on the scan rate preventing the thermodynamic analysis of the unfolding process. In parallel, small conformational changes between wild type and mutant plastocyanin emerge from fluorescence spectroscopy measurements. Here, a difference in the interaction of the two proteins between the microenvironment surrounding the fluorophores and the solvent was proposed. The destabilization observed in the disulfide containing mutant of plastocyanin suggests that the double mutation, Ile21Cys and Glu25Cys, introduces strain into the protein which offsets the stabilizing effect expected from the formation of a covalent crosslink.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15501574</PMID><DateCompleted><Year>2005</Year><Month>03</Month><Day>17</Day></DateCompleted><DateRevised><Year>2008</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0301-4622</ISSN><JournalIssue CitedMedium="Print"><Volume>112</Volume><Issue>1</Issue><PubDate><Year>2004</Year><Month>Dec</Month><Day>01</Day></PubDate></JournalIssue><Title>Biophysical chemistry</Title><ISOAbbreviation>Biophys Chem</ISOAbbreviation></Journal><ArticleTitle>Thermal stability of wild type and disulfide bridge containing mutant of poplar plastocyanin.</ArticleTitle><Pagination><MedlinePgn>35-43</MedlinePgn></Pagination><Abstract><AbstractText>A comparative study of the thermal stability of wild type poplar plastocyanin and of a mutant form containing a disulfide bridge between residues 21 and 25 was performed using differential scanning calorimetry and optical spectroscopic techniques. For wild type plastocyanin the transition temperature, determined from the calorimetric profiles, is 62.7 degrees C at the scan rate of 60 degrees C/h, whereas for the mutant it is reduced to 58.0 degrees C. In both cases, the endothermic peak is followed by an exothermic one at higher temperatures. The unfolding process monitored by optical absorption at 596 nm also reveals a reduced thermal stability of the mutated plastocyanin compared to the wild type protein, with transition temperatures of 54.8 and 58.0 degrees C, respectively. For both proteins, the denaturation process was found to be irreversible and dependent on the scan rate preventing the thermodynamic analysis of the unfolding process. In parallel, small conformational changes between wild type and mutant plastocyanin emerge from fluorescence spectroscopy measurements. Here, a difference in the interaction of the two proteins between the microenvironment surrounding the fluorophores and the solvent was proposed. The destabilization observed in the disulfide containing mutant of plastocyanin suggests that the double mutation, Ile21Cys and Glu25Cys, introduces strain into the protein which offsets the stabilizing effect expected from the formation of a covalent crosslink.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Guzzi</LastName><ForeName>Rita</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Dipartimento di Fisica and Unità INFM, Laboratorio di Biofisica Molecolare, Università della Calabria, Ponte P. Bucci, Cubo 31C, 87036 Rende, Italy. guzzi@fis.unical.it</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Andolfi</LastName><ForeName>Laura</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Cannistraro</LastName><ForeName>Salvatore</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Verbeet</LastName><ForeName>Martin Ph</ForeName><Initials>MP</Initials></Author><Author ValidYN="Y"><LastName>Canters</LastName><ForeName>Gerard W</ForeName><Initials>GW</Initials></Author><Author ValidYN="Y"><LastName>Sportelli</LastName><ForeName>Luigi</ForeName><Initials>L</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biophys Chem</MedlineTA><NlmUniqueID>0403171</NlmUniqueID><ISSNLinking>0301-4622</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004220">Disulfides</NameOfSubstance></Chemical><Chemical><RegistryNumber>9014-09-9</RegistryNumber><NameOfSubstance UI="D010970">Plastocyanin</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002152" MajorTopicYN="N">Calorimetry, Differential Scanning</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004220" MajorTopicYN="N">Disulfides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006358" MajorTopicYN="N">Hot Temperature</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010970" MajorTopicYN="N">Plastocyanin</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011489" MajorTopicYN="N">Protein Denaturation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017510" MajorTopicYN="N">Protein Folding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013050" MajorTopicYN="N">Spectrometry, Fluorescence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013816" MajorTopicYN="N">Thermodynamics</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2004</Year><Month>04</Month><Day>27</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2004</Year><Month>06</Month><Day>28</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2004</Year><Month>07</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2004</Year><Month>10</Month><Day>27</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2005</Year><Month>3</Month><Day>18</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2004</Year><Month>10</Month><Day>27</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">15501574</ArticleId><ArticleId IdType="pii">S0301-4622(04)00166-8</ArticleId><ArticleId IdType="doi">10.1016/j.bpc.2004.07.002</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Italie</li></country></list><tree><noCountry><name sortKey="Andolfi, Laura" sort="Andolfi, Laura" uniqKey="Andolfi L" first="Laura" last="Andolfi">Laura Andolfi</name><name sortKey="Cannistraro, Salvatore" sort="Cannistraro, Salvatore" uniqKey="Cannistraro S" first="Salvatore" last="Cannistraro">Salvatore Cannistraro</name><name sortKey="Canters, Gerard W" sort="Canters, Gerard W" uniqKey="Canters G" first="Gerard W" last="Canters">Gerard W. Canters</name><name sortKey="Sportelli, Luigi" sort="Sportelli, Luigi" uniqKey="Sportelli L" first="Luigi" last="Sportelli">Luigi Sportelli</name><name sortKey="Verbeet, Martin Ph" sort="Verbeet, Martin Ph" uniqKey="Verbeet M" first="Martin Ph" last="Verbeet">Martin Ph Verbeet</name></noCountry><country name="Italie"><noRegion><name sortKey="Guzzi, Rita" sort="Guzzi, Rita" uniqKey="Guzzi R" first="Rita" last="Guzzi">Rita Guzzi</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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