Comparative study of the stability of poplar plastocyanin isoforms.
Identifieur interne : 004076 ( Main/Exploration ); précédent : 004075; suivant : 004077Comparative study of the stability of poplar plastocyanin isoforms.
Auteurs : A. Shosheva [Bulgarie] ; A. Donchev ; M. Dimitrov ; G. Kostov ; G. Toromanov ; V. Getov ; E. AlexovSource :
- Biochimica et biophysica acta [ 0006-3002 ] ; 2005.
Descripteurs français
- KwdFr :
- Conformation des protéines (MeSH), Dénaturation des protéines (MeSH), Isoformes de protéines (composition chimique), Isoformes de protéines (métabolisme), Plastocyanine (composition chimique), Plastocyanine (métabolisme), Populus (composition chimique), Température (MeSH), Électricité statique (MeSH).
- MESH :
- composition chimique : Isoformes de protéines, Plastocyanine, Populus.
- métabolisme : Isoformes de protéines, Plastocyanine.
- Conformation des protéines, Dénaturation des protéines, Température, Électricité statique.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Plastocyanin, Protein Isoforms.
- chemical , metabolism : Plastocyanin, Protein Isoforms.
- chemistry : Populus.
- Protein Conformation, Protein Denaturation, Static Electricity, Temperature.
Abstract
The stability of the two isoforms of poplar plastocyanin (PCa and PCb) was studied with differential scanning calorimetry (DSC) technique. It was shown that the thermal unfolding of both isoforms is an irreversible process with two endothermic and one exothermic peaks. The melting temperature of PCb was found to be 1.3+/-0.2 K degrees higher than of PCa, which indicates that PCb is more stable. The enthalpy of unfolding was estimated from the heat capacity curves and was found to be significantly higher for PCb at salt concentration I=0.1 M. In addition, PCb unfolding enthalpy and melting temperature are much more sensitive to the changes in the salt concentration as found in the experiments done at different ionic strength. The experiments were complemented with numerical calculations. The salt effect on the stability was modeled using the X-ray structure of PCa and a homology modeled structure of PCb. It was found, in agreement with the experimental data, that the stability of PCb changes by 4.7 kJ more than PCa, as the salt concentration increases from zero to 0.1 M. Thus, the differences in only 12 amino acid positions between "a" and "b" isoforms result in a measurable difference in the folding enthalpy and a significant difference in the salt dependence. The optimization of the electrostatic energies of PCa and PCb were studied and it was shown that PCb is better electrostatically optimized.
DOI: 10.1016/j.bbapap.2004.12.012
PubMed: 15752700
Affiliations:
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Kostov</name></author><author><name sortKey="Toromanov, G" sort="Toromanov, G" uniqKey="Toromanov G" first="G" last="Toromanov">G. Toromanov</name></author><author><name sortKey="Getov, V" sort="Getov, V" uniqKey="Getov V" first="V" last="Getov">V. Getov</name></author><author><name sortKey="Alexov, E" sort="Alexov, E" uniqKey="Alexov E" first="E" last="Alexov">E. 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Shosheva</name><affiliation wicri:level="1"><nlm:affiliation>Institute of Biophysics, Bulgarian Academy of Sciences, Sofia-1113, Bulgaria.</nlm:affiliation><country xml:lang="fr">Bulgarie</country><wicri:regionArea>Institute of Biophysics, Bulgarian Academy of Sciences, Sofia-1113</wicri:regionArea><wicri:noRegion>Sofia-1113</wicri:noRegion></affiliation></author><author><name sortKey="Donchev, A" sort="Donchev, A" uniqKey="Donchev A" first="A" last="Donchev">A. Donchev</name></author><author><name sortKey="Dimitrov, M" sort="Dimitrov, M" uniqKey="Dimitrov M" first="M" last="Dimitrov">M. Dimitrov</name></author><author><name sortKey="Kostov, G" sort="Kostov, G" uniqKey="Kostov G" first="G" last="Kostov">G. Kostov</name></author><author><name sortKey="Toromanov, G" sort="Toromanov, G" uniqKey="Toromanov G" first="G" last="Toromanov">G. Toromanov</name></author><author><name sortKey="Getov, V" sort="Getov, V" uniqKey="Getov V" first="V" last="Getov">V. Getov</name></author><author><name sortKey="Alexov, E" sort="Alexov, E" uniqKey="Alexov E" first="E" last="Alexov">E. Alexov</name></author></analytic><series><title level="j">Biochimica et biophysica acta</title><idno type="ISSN">0006-3002</idno><imprint><date when="2005" type="published">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Plastocyanin (chemistry)</term><term>Plastocyanin (metabolism)</term><term>Populus (chemistry)</term><term>Protein Conformation (MeSH)</term><term>Protein Denaturation (MeSH)</term><term>Protein Isoforms (chemistry)</term><term>Protein Isoforms (metabolism)</term><term>Static Electricity (MeSH)</term><term>Temperature (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Conformation des protéines (MeSH)</term><term>Dénaturation des protéines (MeSH)</term><term>Isoformes de protéines (composition chimique)</term><term>Isoformes de protéines (métabolisme)</term><term>Plastocyanine (composition chimique)</term><term>Plastocyanine (métabolisme)</term><term>Populus (composition chimique)</term><term>Température (MeSH)</term><term>Électricité statique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Plastocyanin</term><term>Protein Isoforms</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Plastocyanin</term><term>Protein Isoforms</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Populus</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Isoformes de protéines</term><term>Plastocyanine</term><term>Populus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Isoformes de protéines</term><term>Plastocyanine</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Protein Conformation</term><term>Protein Denaturation</term><term>Static Electricity</term><term>Temperature</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Conformation des protéines</term><term>Dénaturation des protéines</term><term>Température</term><term>Électricité statique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The stability of the two isoforms of poplar plastocyanin (PCa and PCb) was studied with differential scanning calorimetry (DSC) technique. It was shown that the thermal unfolding of both isoforms is an irreversible process with two endothermic and one exothermic peaks. The melting temperature of PCb was found to be 1.3+/-0.2 K degrees higher than of PCa, which indicates that PCb is more stable. The enthalpy of unfolding was estimated from the heat capacity curves and was found to be significantly higher for PCb at salt concentration I=0.1 M. In addition, PCb unfolding enthalpy and melting temperature are much more sensitive to the changes in the salt concentration as found in the experiments done at different ionic strength. The experiments were complemented with numerical calculations. The salt effect on the stability was modeled using the X-ray structure of PCa and a homology modeled structure of PCb. It was found, in agreement with the experimental data, that the stability of PCb changes by 4.7 kJ more than PCa, as the salt concentration increases from zero to 0.1 M. Thus, the differences in only 12 amino acid positions between "a" and "b" isoforms result in a measurable difference in the folding enthalpy and a significant difference in the salt dependence. The optimization of the electrostatic energies of PCa and PCb were studied and it was shown that PCb is better electrostatically optimized.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15752700</PMID><DateCompleted><Year>2005</Year><Month>04</Month><Day>28</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>26</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0006-3002</ISSN><JournalIssue CitedMedium="Print"><Volume>1748</Volume><Issue>1</Issue><PubDate><Year>2005</Year><Month>Apr</Month><Day>15</Day></PubDate></JournalIssue><Title>Biochimica et biophysica acta</Title><ISOAbbreviation>Biochim Biophys Acta</ISOAbbreviation></Journal><ArticleTitle>Comparative study of the stability of poplar plastocyanin isoforms.</ArticleTitle><Pagination><MedlinePgn>116-27</MedlinePgn></Pagination><Abstract><AbstractText>The stability of the two isoforms of poplar plastocyanin (PCa and PCb) was studied with differential scanning calorimetry (DSC) technique. It was shown that the thermal unfolding of both isoforms is an irreversible process with two endothermic and one exothermic peaks. The melting temperature of PCb was found to be 1.3+/-0.2 K degrees higher than of PCa, which indicates that PCb is more stable. The enthalpy of unfolding was estimated from the heat capacity curves and was found to be significantly higher for PCb at salt concentration I=0.1 M. In addition, PCb unfolding enthalpy and melting temperature are much more sensitive to the changes in the salt concentration as found in the experiments done at different ionic strength. The experiments were complemented with numerical calculations. The salt effect on the stability was modeled using the X-ray structure of PCa and a homology modeled structure of PCb. It was found, in agreement with the experimental data, that the stability of PCb changes by 4.7 kJ more than PCa, as the salt concentration increases from zero to 0.1 M. Thus, the differences in only 12 amino acid positions between "a" and "b" isoforms result in a measurable difference in the folding enthalpy and a significant difference in the salt dependence. The optimization of the electrostatic energies of PCa and PCb were studied and it was shown that PCb is better electrostatically optimized.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Shosheva</LastName><ForeName>A</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Institute of Biophysics, Bulgarian Academy of Sciences, Sofia-1113, Bulgaria.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Donchev</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Dimitrov</LastName><ForeName>M</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Kostov</LastName><ForeName>G</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Toromanov</LastName><ForeName>G</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Getov</LastName><ForeName>V</ForeName><Initials>V</Initials></Author><Author ValidYN="Y"><LastName>Alexov</LastName><ForeName>E</ForeName><Initials>E</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><ArticleDate DateType="Electronic"><Year>2005</Year><Month>01</Month><Day>11</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biochim Biophys Acta</MedlineTA><NlmUniqueID>0217513</NlmUniqueID><ISSNLinking>0006-3002</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D020033">Protein Isoforms</NameOfSubstance></Chemical><Chemical><RegistryNumber>9014-09-9</RegistryNumber><NameOfSubstance UI="D010970">Plastocyanin</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D010970" MajorTopicYN="N">Plastocyanin</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</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="D020033" MajorTopicYN="N">Protein Isoforms</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D055672" MajorTopicYN="N">Static Electricity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013696" MajorTopicYN="N">Temperature</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2004</Year><Month>10</Month><Day>01</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2004</Year><Month>12</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2004</Year><Month>12</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2005</Year><Month>3</Month><Day>9</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2005</Year><Month>4</Month><Day>29</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2005</Year><Month>3</Month><Day>9</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">15752700</ArticleId><ArticleId IdType="pii">S1570-9639(04)00348-6</ArticleId><ArticleId IdType="doi">10.1016/j.bbapap.2004.12.012</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Bulgarie</li></country></list><tree><noCountry><name sortKey="Alexov, E" sort="Alexov, E" uniqKey="Alexov E" first="E" last="Alexov">E. Alexov</name><name sortKey="Dimitrov, M" sort="Dimitrov, M" uniqKey="Dimitrov M" first="M" last="Dimitrov">M. Dimitrov</name><name sortKey="Donchev, A" sort="Donchev, A" uniqKey="Donchev A" first="A" last="Donchev">A. Donchev</name><name sortKey="Getov, V" sort="Getov, V" uniqKey="Getov V" first="V" last="Getov">V. Getov</name><name sortKey="Kostov, G" sort="Kostov, G" uniqKey="Kostov G" first="G" last="Kostov">G. Kostov</name><name sortKey="Toromanov, G" sort="Toromanov, G" uniqKey="Toromanov G" first="G" last="Toromanov">G. Toromanov</name></noCountry><country name="Bulgarie"><noRegion><name sortKey="Shosheva, A" sort="Shosheva, A" uniqKey="Shosheva A" first="A" last="Shosheva">A. Shosheva</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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