Characterization of backbone dynamics using solution NMR spectroscopy to discern the functional plasticity of structurally analogous proteins
Summary: The comprehensive delineation of inherent dynamic motions embedded in proteins, which can be crucial for their functional repertoire, is often essential yet remains poorly understood in the majority of cases. In this protocol, we outline detailed descriptions of the necessary steps for empl...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
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Elsevier
2021-12-01
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| Series: | STAR Protocols |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2666166721006250 |
| _version_ | 1819174647104536576 |
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| author | Ashish A. Kawale Björn M. Burmann |
| author_facet | Ashish A. Kawale Björn M. Burmann |
| author_sort | Ashish A. Kawale |
| collection | DOAJ |
| description | Summary: The comprehensive delineation of inherent dynamic motions embedded in proteins, which can be crucial for their functional repertoire, is often essential yet remains poorly understood in the majority of cases. In this protocol, we outline detailed descriptions of the necessary steps for employing solution NMR spectroscopy for the in-depth amino acid level understanding of backbone dynamics of proteins. We describe the application of the protocol on the structurally analogous Tudor domains with disparate functionalities as a model system.For complete details on the use and execution of this protocol, please refer to Kawale and Burmann (2021). |
| first_indexed | 2024-12-22T20:42:17Z |
| format | Article |
| id | doaj.art-a61b64126a664d9295b0ffd3bb75ccfc |
| institution | Directory Open Access Journal |
| issn | 2666-1667 |
| language | English |
| last_indexed | 2024-12-22T20:42:17Z |
| publishDate | 2021-12-01 |
| publisher | Elsevier |
| record_format | Article |
| series | STAR Protocols |
| spelling | doaj.art-a61b64126a664d9295b0ffd3bb75ccfc2022-12-21T18:13:19ZengElsevierSTAR Protocols2666-16672021-12-0124100919Characterization of backbone dynamics using solution NMR spectroscopy to discern the functional plasticity of structurally analogous proteinsAshish A. Kawale0Björn M. Burmann1Wallenberg Centre for Molecular and Translational Medicine, University of Gothenburg, 405 30 Gothenburg, Sweden; Department of Chemistry and Molecular Biology, University of Gothenburg, 405 30 Gothenburg, Sweden; Corresponding authorWallenberg Centre for Molecular and Translational Medicine, University of Gothenburg, 405 30 Gothenburg, Sweden; Department of Chemistry and Molecular Biology, University of Gothenburg, 405 30 Gothenburg, Sweden; Corresponding authorSummary: The comprehensive delineation of inherent dynamic motions embedded in proteins, which can be crucial for their functional repertoire, is often essential yet remains poorly understood in the majority of cases. In this protocol, we outline detailed descriptions of the necessary steps for employing solution NMR spectroscopy for the in-depth amino acid level understanding of backbone dynamics of proteins. We describe the application of the protocol on the structurally analogous Tudor domains with disparate functionalities as a model system.For complete details on the use and execution of this protocol, please refer to Kawale and Burmann (2021).http://www.sciencedirect.com/science/article/pii/S2666166721006250BiophysicsProtein BiochemistryStructural BiologyNMR |
| spellingShingle | Ashish A. Kawale Björn M. Burmann Characterization of backbone dynamics using solution NMR spectroscopy to discern the functional plasticity of structurally analogous proteins STAR Protocols Biophysics Protein Biochemistry Structural Biology NMR |
| title | Characterization of backbone dynamics using solution NMR spectroscopy to discern the functional plasticity of structurally analogous proteins |
| title_full | Characterization of backbone dynamics using solution NMR spectroscopy to discern the functional plasticity of structurally analogous proteins |
| title_fullStr | Characterization of backbone dynamics using solution NMR spectroscopy to discern the functional plasticity of structurally analogous proteins |
| title_full_unstemmed | Characterization of backbone dynamics using solution NMR spectroscopy to discern the functional plasticity of structurally analogous proteins |
| title_short | Characterization of backbone dynamics using solution NMR spectroscopy to discern the functional plasticity of structurally analogous proteins |
| title_sort | characterization of backbone dynamics using solution nmr spectroscopy to discern the functional plasticity of structurally analogous proteins |
| topic | Biophysics Protein Biochemistry Structural Biology NMR |
| url | http://www.sciencedirect.com/science/article/pii/S2666166721006250 |
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