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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The complexity of protein energy landscapes studied by solution NMR relaxation dispersion experiments</title><author><name sortKey="Khirich, Gennady" sort="Khirich, Gennady" uniqKey="Khirich G" first="Gennady" last="Khirich">Gennady Khirich</name><affiliation><nlm:aff id="A1">Department of Chemistry, 225 Prospect Street, New Haven, CT 06520</nlm:aff></affiliation></author><author><name sortKey="Loria, J Patrick" sort="Loria, J Patrick" uniqKey="Loria J" first="J. Patrick" last="Loria">J. Patrick Loria</name><affiliation><nlm:aff id="A1">Department of Chemistry, 225 Prospect Street, New Haven, CT 06520</nlm:aff></affiliation><affiliation><nlm:aff id="A2">Department of Molecular Biophysics and Biochemistry, 260 Whitney Avenue, New Haven, CT 06520</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">25680027</idno><idno type="pmc">4710144</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4710144</idno><idno type="RBID">PMC:4710144</idno><idno type="doi">10.1021/acs.jpcb.5b00212</idno><date when="2015">2015</date><idno type="wicri:Area/Pmc/Corpus">000099</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000099</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">The complexity of protein energy landscapes studied by solution NMR relaxation dispersion experiments</title><author><name sortKey="Khirich, Gennady" sort="Khirich, Gennady" uniqKey="Khirich G" first="Gennady" last="Khirich">Gennady Khirich</name><affiliation><nlm:aff id="A1">Department of Chemistry, 225 Prospect Street, New Haven, CT 06520</nlm:aff></affiliation></author><author><name sortKey="Loria, J Patrick" sort="Loria, J Patrick" uniqKey="Loria J" first="J. Patrick" last="Loria">J. Patrick Loria</name><affiliation><nlm:aff id="A1">Department of Chemistry, 225 Prospect Street, New Haven, CT 06520</nlm:aff></affiliation><affiliation><nlm:aff id="A2">Department of Molecular Biophysics and Biochemistry, 260 Whitney Avenue, New Haven, CT 06520</nlm:aff></affiliation></author></analytic><series><title level="j">The journal of physical chemistry. B</title><idno type="ISSN">1520-6106</idno><idno type="eISSN">1520-5207</idno><imprint><date when="2015">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p id="P1">The millisecond timescale motions in ribonuclease A (RNase A) were studied by solution NMR CPMG and off-resonance R<sub>1ρ</sub> relaxation dispersion experiments over a wide pH and temperature range. These experiments identify three separate protein regions termed Cluster 1, Cluster 2, and R33 whose motions are governed by distinct thermodynamic parameters. Moreover each of these regions has motions with different pH dependencies. Cluster 1 shows an increase in activation enthalpy and activation entropy as the pH is lowered, whereas Cluster two exhibits the opposite behavior. In contrast the activation enthalpy and entropy of R33 show no pH dependence. Compounding the differences, Δω values for Cluster 2 are characteristic of two-site conformational exchange yet similar analysis for Cluster 1 indicates that this region of the enzyme exhibits conformational fluctuations between a major conformer and a pH-dependent average of protonated and de-protonated minor conformers.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<pmc-dir>properties manuscript</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-journal-id">101157530</journal-id><journal-id journal-id-type="pubmed-jr-id">30073</journal-id><journal-id journal-id-type="nlm-ta">J Phys Chem B</journal-id><journal-id journal-id-type="iso-abbrev">J Phys Chem B</journal-id><journal-title-group><journal-title>The journal of physical chemistry. B</journal-title></journal-title-group><issn pub-type="ppub">1520-6106</issn><issn pub-type="epub">1520-5207</issn></journal-meta><article-meta><article-id pub-id-type="pmid">25680027</article-id><article-id pub-id-type="pmc">4710144</article-id><article-id pub-id-type="doi">10.1021/acs.jpcb.5b00212</article-id><article-id pub-id-type="manuscript">NIHMS732342</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>The complexity of protein energy landscapes studied by solution NMR relaxation dispersion experiments</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Khirich</surname><given-names>Gennady</given-names></name><xref ref-type="aff" rid="A1">1</xref></contrib><contrib contrib-type="author"><name><surname>Loria</surname><given-names>J. Patrick</given-names></name><xref ref-type="aff" rid="A1">1</xref><xref ref-type="aff" rid="A2">2</xref><xref ref-type="corresp" rid="cor1">*</xref></contrib></contrib-group><aff id="A1"><label>1</label>Department of Chemistry, 225 Prospect Street, New Haven, CT 06520</aff><aff id="A2"><label>2</label>Department of Molecular Biophysics and Biochemistry, 260 Whitney Avenue, New Haven, CT 06520</aff><author-notes><corresp id="cor1"><label>*</label><bold>Corresponding Author</bold>, <email>patrick.loria@yale.edu</email>. Phone: (203)-436-2518. Fax: (203)-432-6144</corresp></author-notes><pub-date pub-type="nihms-submitted"><day>6</day><month>1</month><year>2016</year></pub-date><pub-date pub-type="epub"><day>20</day><month>2</month><year>2015</year></pub-date><pub-date pub-type="ppub"><day>5</day><month>3</month><year>2015</year></pub-date><pub-date pub-type="pmc-release"><day>05</day><month>3</month><year>2016</year></pub-date><volume>119</volume><issue>9</issue><fpage>3743</fpage><lpage>3754</lpage><pmc-comment>elocation-id from pubmed: 10.1021/acs.jpcb.5b00212</pmc-comment>
<abstract><p id="P1">The millisecond timescale motions in ribonuclease A (RNase A) were studied by solution NMR CPMG and off-resonance R<sub>1ρ</sub> relaxation dispersion experiments over a wide pH and temperature range. These experiments identify three separate protein regions termed Cluster 1, Cluster 2, and R33 whose motions are governed by distinct thermodynamic parameters. Moreover each of these regions has motions with different pH dependencies. Cluster 1 shows an increase in activation enthalpy and activation entropy as the pH is lowered, whereas Cluster two exhibits the opposite behavior. In contrast the activation enthalpy and entropy of R33 show no pH dependence. Compounding the differences, Δω values for Cluster 2 are characteristic of two-site conformational exchange yet similar analysis for Cluster 1 indicates that this region of the enzyme exhibits conformational fluctuations between a major conformer and a pH-dependent average of protonated and de-protonated minor conformers.</p></abstract><kwd-group><kwd>NMR</kwd><kwd>protein dynamics</kwd><kwd>enzyme</kwd><kwd>relaxation dispersion</kwd><kwd>rotating frame relaxation</kwd></kwd-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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