Electronic structures of Ascaris trypsin inhibitor in solution.
Identifieur interne : 000517 ( Ncbi/Merge ); précédent : 000516; suivant : 000518Electronic structures of Ascaris trypsin inhibitor in solution.
Auteurs : Haoping Zheng [République populaire de Chine]Source :
- Physical review. E, Statistical, nonlinear, and soft matter physics [ 1539-3755 ] ; 2003.
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Abstract
The electronic structures of Ascaris trypsin inhibitor in solution are obtained by the first-principles, all-electron, ab initio calculation using the self-consistent cluster-embedding (SCCE) method. The inhibitor, made up of 62 amino acid residues with 912 atoms, has two three-dimensional solution structures: 1ata and 1atb. The calculated ground-state energy of structure 1atb is lower than that of structure 1ata by 6.12 eV. The active sites are determined and explained: only structure 1atb has a N terminal at residue ARG+31. This shows that the structure 1atb is the stable and active form of the inhibitor, which is in agreement with the experimental results. The calculation reveals that some parts of the inhibitor can be easily changed while the inhibitor's biological activity may be kept. This kind of information may be helpful in fighting viruses such as AIDS, SARS, and flu, since these viruses have higher variability. The calculation offers an independent theoretical estimate of the precision of structure determination.
DOI: 10.1103/PhysRevE.68.051908
PubMed: 14682821
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E, Statistical, nonlinear, and soft matter physics</title><idno type="ISSN">1539-3755</idno><imprint><date when="2003" type="published">2003</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Ascaris (metabolism)</term><term>Binding Sites</term><term>Electrons</term><term>Image Processing, Computer-Assisted</term><term>Models, Molecular</term><term>Models, Statistical</term><term>Protein Structure, Tertiary</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Ascaris (métabolisme)</term><term>Modèles moléculaires</term><term>Modèles statistiques</term><term>Sites de fixation</term><term>Structure tertiaire des protéines</term><term>Traitement d'image par ordinateur</term><term>Électrons</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Ascaris</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Ascaris</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Binding Sites</term><term>Electrons</term><term>Image Processing, Computer-Assisted</term><term>Models, Molecular</term><term>Models, Statistical</term><term>Protein Structure, Tertiary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Modèles moléculaires</term><term>Modèles statistiques</term><term>Sites de fixation</term><term>Structure tertiaire des protéines</term><term>Traitement d'image par ordinateur</term><term>Électrons</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The electronic structures of Ascaris trypsin inhibitor in solution are obtained by the first-principles, all-electron, ab initio calculation using the self-consistent cluster-embedding (SCCE) method. The inhibitor, made up of 62 amino acid residues with 912 atoms, has two three-dimensional solution structures: 1ata and 1atb. The calculated ground-state energy of structure 1atb is lower than that of structure 1ata by 6.12 eV. The active sites are determined and explained: only structure 1atb has a N terminal at residue ARG+31. This shows that the structure 1atb is the stable and active form of the inhibitor, which is in agreement with the experimental results. The calculation reveals that some parts of the inhibitor can be easily changed while the inhibitor's biological activity may be kept. This kind of information may be helpful in fighting viruses such as AIDS, SARS, and flu, since these viruses have higher variability. The calculation offers an independent theoretical estimate of the precision of structure determination.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">14682821</PMID><DateCompleted><Year>2004</Year><Month>06</Month><Day>02</Day></DateCompleted><DateRevised><Year>2006</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">1539-3755</ISSN><JournalIssue CitedMedium="Print"><Volume>68</Volume><Issue>5 Pt 1</Issue><PubDate><Year>2003</Year><Month>Nov</Month></PubDate></JournalIssue><Title>Physical review. E, Statistical, nonlinear, and soft matter physics</Title><ISOAbbreviation>Phys Rev E Stat Nonlin Soft Matter Phys</ISOAbbreviation></Journal><ArticleTitle>Electronic structures of Ascaris trypsin inhibitor in solution.</ArticleTitle><Pagination><MedlinePgn>051908</MedlinePgn></Pagination><Abstract><AbstractText>The electronic structures of Ascaris trypsin inhibitor in solution are obtained by the first-principles, all-electron, ab initio calculation using the self-consistent cluster-embedding (SCCE) method. The inhibitor, made up of 62 amino acid residues with 912 atoms, has two three-dimensional solution structures: 1ata and 1atb. The calculated ground-state energy of structure 1atb is lower than that of structure 1ata by 6.12 eV. The active sites are determined and explained: only structure 1atb has a N terminal at residue ARG+31. This shows that the structure 1atb is the stable and active form of the inhibitor, which is in agreement with the experimental results. The calculation reveals that some parts of the inhibitor can be easily changed while the inhibitor's biological activity may be kept. This kind of information may be helpful in fighting viruses such as AIDS, SARS, and flu, since these viruses have higher variability. The calculation offers an independent theoretical estimate of the precision of structure determination.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zheng</LastName><ForeName>Haoping</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Pohl Institute of Solid State Physics, Tongji University, Shanghai 200092, China. zhenghp@mail.tongji.edu.cn</Affiliation></AffiliationInfo></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>2003</Year><Month>11</Month><Day>25</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Phys Rev E Stat Nonlin Soft Matter Phys</MedlineTA><NlmUniqueID>101136452</NlmUniqueID><ISSNLinking>1539-3755</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001200" MajorTopicYN="N">Ascaris</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004583" MajorTopicYN="N">Electrons</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007091" MajorTopicYN="N">Image Processing, Computer-Assisted</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015233" MajorTopicYN="N">Models, Statistical</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2003</Year><Month>07</Month><Day>11</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2003</Year><Month>12</Month><Day>20</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2004</Year><Month>6</Month><Day>3</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2003</Year><Month>12</Month><Day>20</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">14682821</ArticleId><ArticleId IdType="doi">10.1103/PhysRevE.68.051908</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>République populaire de Chine</li></country></list><tree><country name="République populaire de Chine"><noRegion><name sortKey="Zheng, Haoping" sort="Zheng, Haoping" uniqKey="Zheng H" first="Haoping" last="Zheng">Haoping Zheng</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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