Paramagnetic relaxation enhancement for the characterization of the conformational heterogeneity in two-domain proteins.
Identifieur interne : 000715 ( Main/Curation ); précédent : 000714; suivant : 000716Paramagnetic relaxation enhancement for the characterization of the conformational heterogeneity in two-domain proteins.
Auteurs : Ivano Bertini [Italie] ; Claudio Luchinat ; Malini Nagulapalli ; Giacomo Parigi ; Enrico RaveraSource :
- Physical chemistry chemical physics : PCCP [ 1463-9084 ] ; 2012.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Calmodulin, Gadolinium, Lanthanoid Series Elements.
- methods : Nuclear Magnetic Resonance, Biomolecular.
- Algorithms, Models, Molecular, Protein Conformation, Protein Structure, Tertiary, Temperature.
Abstract
Multidomain proteins are often composed of rigid domains that can reorient in solution more or less freely. Calmodulin (CaM) is a two domain protein which can experience a large degree of conformational freedom thanks to a mobile linker connecting the N-terminal and C-terminal domains of the protein. The maximum occurrences (MOs) of the possible protein conformations have been analyzed using the paramagnetic relaxation enhancements (PREs) induced by a gadolinium(III) ion together with the paramagnetic pseudocontact shift and residual dipolar coupling restraints measured in the presence of terbium(III), thulium(III) or dysprosium(III) ions. The results suggest that the PREs provide complementary information useful for improving the description of the conformational heterogeneity of the protein. The data, acquired at 298 K and at 278 K, suggest that compact conformations are disfavoured by decreasing the temperature.
DOI: 10.1039/c2cp40139h
PubMed: 22622816
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Sacconi 6, 50019 Sesto Fiorentino (FI)</wicri:regionArea><wicri:noRegion>50019 Sesto Fiorentino (FI)</wicri:noRegion></affiliation></author><author><name sortKey="Luchinat, Claudio" sort="Luchinat, Claudio" uniqKey="Luchinat C" first="Claudio" last="Luchinat">Claudio Luchinat</name></author><author><name sortKey="Nagulapalli, Malini" sort="Nagulapalli, Malini" uniqKey="Nagulapalli M" first="Malini" last="Nagulapalli">Malini Nagulapalli</name></author><author><name sortKey="Parigi, Giacomo" sort="Parigi, Giacomo" uniqKey="Parigi G" first="Giacomo" last="Parigi">Giacomo Parigi</name></author><author><name sortKey="Ravera, Enrico" sort="Ravera, Enrico" uniqKey="Ravera E" first="Enrico" last="Ravera">Enrico Ravera</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2012">2012</date><idno type="doi">10.1039/c2cp40139h</idno><idno type="RBID">pubmed:22622816</idno><idno type="pmid">22622816</idno><idno type="wicri:Area/PubMed/Corpus">000363</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000363</idno><idno type="wicri:Area/PubMed/Curation">000363</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000363</idno><idno type="wicri:Area/PubMed/Checkpoint">000363</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000363</idno><idno type="wicri:Area/Ncbi/Merge">000579</idno><idno type="wicri:Area/Ncbi/Curation">000579</idno><idno type="wicri:Area/Ncbi/Checkpoint">000579</idno><idno type="wicri:Area/Main/Merge">000716</idno><idno type="wicri:Area/Main/Curation">000715</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Paramagnetic relaxation enhancement for the characterization of the conformational heterogeneity in two-domain proteins.</title><author><name sortKey="Bertini, Ivano" sort="Bertini, Ivano" uniqKey="Bertini I" first="Ivano" last="Bertini">Ivano Bertini</name><affiliation wicri:level="1"><nlm:affiliation>Magnetic Resonance Center (CERM), University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino (FI), Italy. ivanobertini@cerm.unifi.it</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>Magnetic Resonance Center (CERM), University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino (FI)</wicri:regionArea><wicri:noRegion>50019 Sesto Fiorentino (FI)</wicri:noRegion></affiliation></author><author><name sortKey="Luchinat, Claudio" sort="Luchinat, Claudio" uniqKey="Luchinat C" first="Claudio" last="Luchinat">Claudio Luchinat</name></author><author><name sortKey="Nagulapalli, Malini" sort="Nagulapalli, Malini" uniqKey="Nagulapalli M" first="Malini" last="Nagulapalli">Malini Nagulapalli</name></author><author><name sortKey="Parigi, Giacomo" sort="Parigi, Giacomo" uniqKey="Parigi G" first="Giacomo" last="Parigi">Giacomo Parigi</name></author><author><name sortKey="Ravera, Enrico" sort="Ravera, Enrico" uniqKey="Ravera E" first="Enrico" last="Ravera">Enrico Ravera</name></author></analytic><series><title level="j">Physical chemistry chemical physics : PCCP</title><idno type="eISSN">1463-9084</idno><imprint><date when="2012" type="published">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Algorithms</term><term>Calmodulin (chemistry)</term><term>Gadolinium (chemistry)</term><term>Lanthanoid Series Elements (chemistry)</term><term>Models, Molecular</term><term>Nuclear Magnetic Resonance, Biomolecular (methods)</term><term>Protein Conformation</term><term>Protein Structure, Tertiary</term><term>Temperature</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Algorithmes</term><term>Calmoduline ()</term><term>Conformation des protéines</term><term>Gadolinium ()</term><term>Lanthanides ()</term><term>Modèles moléculaires</term><term>Résonance magnétique nucléaire biomoléculaire ()</term><term>Structure tertiaire des protéines</term><term>Température</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Calmodulin</term><term>Gadolinium</term><term>Lanthanoid Series Elements</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Nuclear Magnetic Resonance, Biomolecular</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Algorithms</term><term>Models, Molecular</term><term>Protein Conformation</term><term>Protein Structure, Tertiary</term><term>Temperature</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Algorithmes</term><term>Calmoduline</term><term>Conformation des protéines</term><term>Gadolinium</term><term>Lanthanides</term><term>Modèles moléculaires</term><term>Résonance magnétique nucléaire biomoléculaire</term><term>Structure tertiaire des protéines</term><term>Température</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Multidomain proteins are often composed of rigid domains that can reorient in solution more or less freely. Calmodulin (CaM) is a two domain protein which can experience a large degree of conformational freedom thanks to a mobile linker connecting the N-terminal and C-terminal domains of the protein. The maximum occurrences (MOs) of the possible protein conformations have been analyzed using the paramagnetic relaxation enhancements (PREs) induced by a gadolinium(III) ion together with the paramagnetic pseudocontact shift and residual dipolar coupling restraints measured in the presence of terbium(III), thulium(III) or dysprosium(III) ions. The results suggest that the PREs provide complementary information useful for improving the description of the conformational heterogeneity of the protein. The data, acquired at 298 K and at 278 K, suggest that compact conformations are disfavoured by decreasing the temperature.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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