The complexity of protein energy landscapes studied by solution NMR relaxation dispersion experiments
Identifieur interne : 000741 ( Main/Exploration ); précédent : 000740; suivant : 000742The complexity of protein energy landscapes studied by solution NMR relaxation dispersion experiments
Auteurs : Gennady Khirich [États-Unis] ; J. Patrick Loria [États-Unis]Source :
- The journal of physical chemistry. B [ 1520-6106 ] ; 2015.
Abstract
The millisecond timescale motions in ribonuclease A (RNase A) were studied by solution NMR CPMG and off-resonance R1ρ 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.
Url:
DOI: 10.1021/acs.jpcb.5b00212
PubMed: 25680027
PubMed Central: 4710144
Affiliations:
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Patrick" last="Loria">J. Patrick Loria</name><affiliation wicri:level="2"><nlm:aff id="A1">Department of Chemistry, 225 Prospect Street, New Haven, CT 06520</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Connecticut</region></placeName><wicri:cityArea>Department of Chemistry, 225 Prospect Street, New Haven</wicri:cityArea></affiliation><affiliation wicri:level="2"><nlm:aff id="A2">Department of Molecular Biophysics and Biochemistry, 260 Whitney Avenue, New Haven, CT 06520</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Connecticut</region></placeName><wicri:cityArea>Department of Molecular Biophysics and Biochemistry, 260 Whitney Avenue, New Haven</wicri:cityArea></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><affiliations><list><country><li>États-Unis</li></country><region><li>Connecticut</li></region></list><tree><country name="États-Unis"><region name="Connecticut"><name sortKey="Khirich, Gennady" sort="Khirich, Gennady" uniqKey="Khirich G" first="Gennady" last="Khirich">Gennady Khirich</name></region><name sortKey="Loria, J Patrick" sort="Loria, J Patrick" uniqKey="Loria J" first="J. Patrick" last="Loria">J. Patrick Loria</name><name sortKey="Loria, J Patrick" sort="Loria, J Patrick" uniqKey="Loria J" first="J. Patrick" last="Loria">J. Patrick Loria</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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