Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions
Intrinsically disordered linkers provide multi-domain proteins with degrees of conformational freedom that are often essential for function. These highly dynamic assemblies represent a significant fraction of all proteomes, and deciphering the physical basis of their interactions represents a consid...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2016-09-01
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| Series: | Frontiers in Molecular Biosciences |
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| Online Access: | http://journal.frontiersin.org/Journal/10.3389/fmolb.2016.00054/full |
| _version_ | 1819213125552963584 |
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| author | Elise Delaforge Sigrid Milles Jie-rong Huang Denis Bouvier Malene Ringkjøbing Jensen Darren Hart Michael Sattler Michael Sattler Martin Blackledge |
| author_facet | Elise Delaforge Sigrid Milles Jie-rong Huang Denis Bouvier Malene Ringkjøbing Jensen Darren Hart Michael Sattler Michael Sattler Martin Blackledge |
| author_sort | Elise Delaforge |
| collection | DOAJ |
| description | Intrinsically disordered linkers provide multi-domain proteins with degrees of conformational freedom that are often essential for function. These highly dynamic assemblies represent a significant fraction of all proteomes, and deciphering the physical basis of their interactions represents a considerable challenge. Here we describe the difficulties associated with mapping the large-scale domain dynamics and describe two recent examples where solution state methods, in particular NMR spectroscopy, are used to investigate conformational exchange on very different timescales. |
| first_indexed | 2024-12-23T06:53:53Z |
| format | Article |
| id | doaj.art-9537d8253b004956ad2b6d6e21dfa9a2 |
| institution | Directory Open Access Journal |
| issn | 2296-889X |
| language | English |
| last_indexed | 2024-12-23T06:53:53Z |
| publishDate | 2016-09-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Molecular Biosciences |
| spelling | doaj.art-9537d8253b004956ad2b6d6e21dfa9a22022-12-21T17:56:22ZengFrontiers Media S.A.Frontiers in Molecular Biosciences2296-889X2016-09-01310.3389/fmolb.2016.00054218036Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein InteractionsElise Delaforge0Sigrid Milles1Jie-rong Huang2Denis Bouvier3Malene Ringkjøbing Jensen4Darren Hart5Michael Sattler6Michael Sattler7Martin Blackledge8Institut de Biologie Structurale, Univ. Grenoble Alpes, CNRS, CEAInstitut de Biologie Structurale, Univ. Grenoble Alpes, CNRS, CEAInstitut de Biologie Structurale, Univ. Grenoble Alpes, CNRS, CEAInstitut de Biologie Structurale, Univ. Grenoble Alpes, CNRS, CEAInstitut de Biologie Structurale, Univ. Grenoble Alpes, CNRS, CEAInstitut de Biologie Structurale, Univ. Grenoble Alpes, CNRS, CEAInstitute of Structural Biology, Helmholtz Zentrum MünchenCenter for Integrated Protein Science Munich at Biomolecular NMRInstitut de Biologie Structurale, Univ. Grenoble Alpes, CNRS, CEAIntrinsically disordered linkers provide multi-domain proteins with degrees of conformational freedom that are often essential for function. These highly dynamic assemblies represent a significant fraction of all proteomes, and deciphering the physical basis of their interactions represents a considerable challenge. Here we describe the difficulties associated with mapping the large-scale domain dynamics and describe two recent examples where solution state methods, in particular NMR spectroscopy, are used to investigate conformational exchange on very different timescales.http://journal.frontiersin.org/Journal/10.3389/fmolb.2016.00054/fullNuclear Magnetic ResonanceproteinConformational selectionSmall-angle scatteringChemical exchange saturation transfer (CEST)conformational dynamics |
| spellingShingle | Elise Delaforge Sigrid Milles Jie-rong Huang Denis Bouvier Malene Ringkjøbing Jensen Darren Hart Michael Sattler Michael Sattler Martin Blackledge Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions Frontiers in Molecular Biosciences Nuclear Magnetic Resonance protein Conformational selection Small-angle scattering Chemical exchange saturation transfer (CEST) conformational dynamics |
| title | Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions |
| title_full | Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions |
| title_fullStr | Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions |
| title_full_unstemmed | Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions |
| title_short | Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions |
| title_sort | investigating the role of large scale domain dynamics in protein protein interactions |
| topic | Nuclear Magnetic Resonance protein Conformational selection Small-angle scattering Chemical exchange saturation transfer (CEST) conformational dynamics |
| url | http://journal.frontiersin.org/Journal/10.3389/fmolb.2016.00054/full |
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