Recognition Dynamics up to Microseconds Revealed from an RDC-Derived Ubiquitin Ensemble in Solution
Protein dynamics are essential for protein function, and yet it has been challenging to access the underlying atomic motions in solution on nanosecond-to-microsecond time scales. We present a structural ensemble of ubiquitin, refined against residual dipolar couplings (RDCs), comprising solution dyn...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 2008-06, Vol.320 (5882), p.1471-1475 |
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| creator | Lange, Oliver F. Lakomek, Nils-Alexander Farès, Christophe Schröder, Gunnar F. Walter, Korvin F. A. Becker, Stefan Meiler, Jens Grubmüller, Helmut Griesinger, Christian de Groot, Bert L. |
| description | Protein dynamics are essential for protein function, and yet it has been challenging to access the underlying atomic motions in solution on nanosecond-to-microsecond time scales. We present a structural ensemble of ubiquitin, refined against residual dipolar couplings (RDCs), comprising solution dynamics up to microseconds. The ensemble covers the complete structural heterogeneity observed in 46 ubiquitin crystal structures, most of which are complexes with other proteins. Conformational selection, rather than induced-fit motion, thus suffices to explain the molecular recognition dynamics of ubiquitin. Marked correlations are seen between the flexibility of the ensemble and contacts formed in ubiquitin complexes. A large part of the solution dynamics is concentrated in one concerted mode, which accounts for most of ubiquitin's molecular recognition heterogeneity and ensures a low entropic complex formation cost. |
| doi_str_mv | 10.1126/science.1157092 |
| format | Article |
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A. ; Becker, Stefan ; Meiler, Jens ; Grubmüller, Helmut ; Griesinger, Christian ; de Groot, Bert L.</creator><creatorcontrib>Lange, Oliver F. ; Lakomek, Nils-Alexander ; Farès, Christophe ; Schröder, Gunnar F. ; Walter, Korvin F. A. ; Becker, Stefan ; Meiler, Jens ; Grubmüller, Helmut ; Griesinger, Christian ; de Groot, Bert L.</creatorcontrib><description>Protein dynamics are essential for protein function, and yet it has been challenging to access the underlying atomic motions in solution on nanosecond-to-microsecond time scales. We present a structural ensemble of ubiquitin, refined against residual dipolar couplings (RDCs), comprising solution dynamics up to microseconds. The ensemble covers the complete structural heterogeneity observed in 46 ubiquitin crystal structures, most of which are complexes with other proteins. Conformational selection, rather than induced-fit motion, thus suffices to explain the molecular recognition dynamics of ubiquitin. Marked correlations are seen between the flexibility of the ensemble and contacts formed in ubiquitin complexes. A large part of the solution dynamics is concentrated in one concerted mode, which accounts for most of ubiquitin's molecular recognition heterogeneity and ensures a low entropic complex formation cost.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.1157092</identifier><identifier>PMID: 18556554</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Association for the Advancement of Science</publisher><subject>Amides ; Amino Acid Motifs ; Animals ; Anisotropy ; Biological and medical sciences ; Biophysics ; Chemical Phenomena ; Chemistry, Physical ; Crystal structure ; Crystallography, X-Ray ; Data lines ; Datasets ; Entropy ; Fundamental and applied biological sciences. Psychology ; Geometric lines ; Interactions. Associations ; Intermolecular phenomena ; Kinetics ; Models, Molecular ; Molecular biology ; Molecular biophysics ; Molecular structure ; Nuclear magnetic resonance ; Nuclear Magnetic Resonance, Biomolecular ; Principal components analysis ; Protein Binding ; Protein Conformation ; Protein Structure, Tertiary ; Proteins ; Solutions ; Time ; Ubiquitin - chemistry ; Ubiquitin - metabolism ; Ubiquitins ; Xenopus laevis</subject><ispartof>Science (American Association for the Advancement of Science), 2008-06, Vol.320 (5882), p.1471-1475</ispartof><rights>Copyright 2008 American Association for the Advancement of Science</rights><rights>2008 INIST-CNRS</rights><rights>Copyright © 2008, American Association for the Advancement of Science</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c512t-3285e458c87321759265a3da2e1fd62e23722c53dff5b393c696c8f3f1f76d1d3</citedby><cites>FETCH-LOGICAL-c512t-3285e458c87321759265a3da2e1fd62e23722c53dff5b393c696c8f3f1f76d1d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/20054265$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/20054265$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,777,781,800,2871,2872,27905,27906,57998,58231</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=20448672$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18556554$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lange, Oliver F.</creatorcontrib><creatorcontrib>Lakomek, Nils-Alexander</creatorcontrib><creatorcontrib>Farès, Christophe</creatorcontrib><creatorcontrib>Schröder, Gunnar F.</creatorcontrib><creatorcontrib>Walter, Korvin F. A.</creatorcontrib><creatorcontrib>Becker, Stefan</creatorcontrib><creatorcontrib>Meiler, Jens</creatorcontrib><creatorcontrib>Grubmüller, Helmut</creatorcontrib><creatorcontrib>Griesinger, Christian</creatorcontrib><creatorcontrib>de Groot, Bert L.</creatorcontrib><title>Recognition Dynamics up to Microseconds Revealed from an RDC-Derived Ubiquitin Ensemble in Solution</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>Protein dynamics are essential for protein function, and yet it has been challenging to access the underlying atomic motions in solution on nanosecond-to-microsecond time scales. We present a structural ensemble of ubiquitin, refined against residual dipolar couplings (RDCs), comprising solution dynamics up to microseconds. The ensemble covers the complete structural heterogeneity observed in 46 ubiquitin crystal structures, most of which are complexes with other proteins. Conformational selection, rather than induced-fit motion, thus suffices to explain the molecular recognition dynamics of ubiquitin. Marked correlations are seen between the flexibility of the ensemble and contacts formed in ubiquitin complexes. A large part of the solution dynamics is concentrated in one concerted mode, which accounts for most of ubiquitin's molecular recognition heterogeneity and ensures a low entropic complex formation cost.</description><subject>Amides</subject><subject>Amino Acid Motifs</subject><subject>Animals</subject><subject>Anisotropy</subject><subject>Biological and medical sciences</subject><subject>Biophysics</subject><subject>Chemical Phenomena</subject><subject>Chemistry, Physical</subject><subject>Crystal structure</subject><subject>Crystallography, X-Ray</subject><subject>Data lines</subject><subject>Datasets</subject><subject>Entropy</subject><subject>Fundamental and applied biological sciences. 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A.</au><au>Becker, Stefan</au><au>Meiler, Jens</au><au>Grubmüller, Helmut</au><au>Griesinger, Christian</au><au>de Groot, Bert L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Recognition Dynamics up to Microseconds Revealed from an RDC-Derived Ubiquitin Ensemble in Solution</atitle><jtitle>Science (American Association for the Advancement of Science)</jtitle><addtitle>Science</addtitle><date>2008-06-13</date><risdate>2008</risdate><volume>320</volume><issue>5882</issue><spage>1471</spage><epage>1475</epage><pages>1471-1475</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><coden>SCIEAS</coden><abstract>Protein dynamics are essential for protein function, and yet it has been challenging to access the underlying atomic motions in solution on nanosecond-to-microsecond time scales. We present a structural ensemble of ubiquitin, refined against residual dipolar couplings (RDCs), comprising solution dynamics up to microseconds. The ensemble covers the complete structural heterogeneity observed in 46 ubiquitin crystal structures, most of which are complexes with other proteins. Conformational selection, rather than induced-fit motion, thus suffices to explain the molecular recognition dynamics of ubiquitin. Marked correlations are seen between the flexibility of the ensemble and contacts formed in ubiquitin complexes. A large part of the solution dynamics is concentrated in one concerted mode, which accounts for most of ubiquitin's molecular recognition heterogeneity and ensures a low entropic complex formation cost.</abstract><cop>Washington, DC</cop><pub>American Association for the Advancement of Science</pub><pmid>18556554</pmid><doi>10.1126/science.1157092</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Science (American Association for the Advancement of Science), 2008-06, Vol.320 (5882), p.1471-1475 |
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| subjects | Amides Amino Acid Motifs Animals Anisotropy Biological and medical sciences Biophysics Chemical Phenomena Chemistry, Physical Crystal structure Crystallography, X-Ray Data lines Datasets Entropy Fundamental and applied biological sciences. Psychology Geometric lines Interactions. Associations Intermolecular phenomena Kinetics Models, Molecular Molecular biology Molecular biophysics Molecular structure Nuclear magnetic resonance Nuclear Magnetic Resonance, Biomolecular Principal components analysis Protein Binding Protein Conformation Protein Structure, Tertiary Proteins Solutions Time Ubiquitin - chemistry Ubiquitin - metabolism Ubiquitins Xenopus laevis |
| title | Recognition Dynamics up to Microseconds Revealed from an RDC-Derived Ubiquitin Ensemble in Solution |
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