Long-range correlated dynamics in intrinsically disordered proteins.
Identifieur interne : 000226 ( Hal/Checkpoint ); précédent : 000225; suivant : 000227Long-range correlated dynamics in intrinsically disordered proteins.
Auteurs : Giacomo Parigi ; Nasrollah Rezaei-Ghaleh ; Andrea Giachetti [Italie] ; Stefan Becker ; Claudio Fernandez [France] ; Martin Blackledge [France] ; Christian Griesinger [Allemagne] ; Markus Zweckstetter ; Claudio LuchinatSource :
- Journal of the American Chemical Society [ 0002-7863 ] ; 2014-11-19.
Abstract
Intrinsically disordered proteins (IDPs) are involved in a wide variety of physiological and pathological processes and are best described by ensembles of rapidly interconverting conformers. Using fast field cycling relaxation measurements we here show that the IDP α-synuclein as well as a variety of other IDPs undergoes slow reorientations at time scales comparable to folded proteins. The slow motions are not perturbed by mutations in α-synuclein, which are related to genetic forms of Parkinson's disease, and do not depend on secondary and tertiary structural propensities. Ensemble-based hydrodynamic calculations suggest that the time scale of the underlying correlated motion is largely determined by hydrodynamic coupling between locally rigid segments. Our study indicates that long-range correlated dynamics are an intrinsic property of IDPs and offers a general physical mechanism of correlated motions in highly flexible biomolecular systems.
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<front><div type="abstract" xml:lang="en">Intrinsically disordered proteins (IDPs) are involved in a wide variety of physiological and pathological processes and are best described by ensembles of rapidly interconverting conformers. Using fast field cycling relaxation measurements we here show that the IDP α-synuclein as well as a variety of other IDPs undergoes slow reorientations at time scales comparable to folded proteins. The slow motions are not perturbed by mutations in α-synuclein, which are related to genetic forms of Parkinson's disease, and do not depend on secondary and tertiary structural propensities. Ensemble-based hydrodynamic calculations suggest that the time scale of the underlying correlated motion is largely determined by hydrodynamic coupling between locally rigid segments. Our study indicates that long-range correlated dynamics are an intrinsic property of IDPs and offers a general physical mechanism of correlated motions in highly flexible biomolecular systems.</div>
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<idno type="stamp" n="UNIV-GRENOBLE1" p="UGA">Université Joseph Fourier - Grenoble I</idno>
<idno type="stamp" n="IBS" p="UNIV-GRENOBLE1">Institut de Biologie Structurale</idno>
<idno type="stamp" n="IBS-FDP" p="IBS">Groupe Flexibilité et Dynamique des Protéines par RMN / Protein Dynamics and Flexibility by NMR Group (IBS-FDP)</idno>
<idno type="stamp" n="INRA">INRA - Institut national de la recherche agronomique</idno>
<idno type="stamp" n="FRANCE-GRILLES">France Grilles</idno>
<idno type="stamp" n="DSV" p="CEA">Direction des sciences du vivant</idno>
</seriesStmt>
<notesStmt> <note type="audience" n="2">International</note>
<note type="popular" n="0">No</note>
<note type="peer" n="1">Yes</note>
</notesStmt>
<sourceDesc> <biblStruct> <analytic> <title xml:lang="en">Long-range correlated dynamics in intrinsically disordered proteins.</title>
<author role="aut"> <persName> <forename type="first">Giacomo</forename>
<surname>Parigi</surname>
</persName>
<idno type="halauthorid">1143886</idno>
</author>
<author role="aut"> <persName> <forename type="first">Nasrollah</forename>
<surname>Rezaei-Ghaleh</surname>
</persName>
<idno type="halauthorid">1143887</idno>
</author>
<author role="aut"> <persName> <forename type="first">Andrea</forename>
<surname>Giachetti</surname>
</persName>
<idno type="halauthorid">724833</idno>
<affiliation ref="#struct-114824"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">Stefan</forename>
<surname>Becker</surname>
</persName>
<idno type="halauthorid">414007</idno>
</author>
<author role="aut"> <persName> <forename type="first">Claudio</forename>
<surname>Fernandez</surname>
</persName>
<idno type="halauthorid">690504</idno>
<affiliation ref="#struct-414133"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">Martin</forename>
<surname>Blackledge</surname>
</persName>
<idno type="halauthorid">365922</idno>
<affiliation ref="#struct-576"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">Christian</forename>
<surname>Griesinger</surname>
</persName>
<idno type="halauthorid">1106566</idno>
<affiliation ref="#struct-218741"></affiliation>
</author>
<author role="aut"> <persName> <forename type="first">Markus</forename>
<surname>Zweckstetter</surname>
</persName>
<idno type="halauthorid">1143888</idno>
</author>
<author role="aut"> <persName> <forename type="first">Claudio</forename>
<surname>Luchinat</surname>
</persName>
<idno type="halauthorid">1143889</idno>
</author>
</analytic>
<monogr> <idno type="halJournalId" status="VALID">6500</idno>
<idno type="issn">0002-7863</idno>
<idno type="eissn">1520-5126</idno>
<title level="j">Journal of the American Chemical Society</title>
<imprint> <publisher>American Chemical Society</publisher>
<biblScope unit="volume">136</biblScope>
<biblScope unit="issue">46</biblScope>
<biblScope unit="pp">16201-9</biblScope>
<date type="datePub">2014-11-19</date>
</imprint>
</monogr>
<idno type="pubmed">25331250</idno>
</biblStruct>
</sourceDesc>
<profileDesc> <langUsage> <language ident="en">English</language>
</langUsage>
<textClass> <classCode scheme="halDomain" n="sdv.bbm.bs">Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM]</classCode>
<classCode scheme="halTypology" n="ART">Journal articles</classCode>
</textClass>
<abstract xml:lang="en">Intrinsically disordered proteins (IDPs) are involved in a wide variety of physiological and pathological processes and are best described by ensembles of rapidly interconverting conformers. Using fast field cycling relaxation measurements we here show that the IDP α-synuclein as well as a variety of other IDPs undergoes slow reorientations at time scales comparable to folded proteins. The slow motions are not perturbed by mutations in α-synuclein, which are related to genetic forms of Parkinson's disease, and do not depend on secondary and tertiary structural propensities. Ensemble-based hydrodynamic calculations suggest that the time scale of the underlying correlated motion is largely determined by hydrodynamic coupling between locally rigid segments. Our study indicates that long-range correlated dynamics are an intrinsic property of IDPs and offers a general physical mechanism of correlated motions in highly flexible biomolecular systems.</abstract>
</profileDesc>
</hal>
</record>
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