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Characterization of backbone dynamics using solution NMR spectroscopy to discern the functional plasticity of structurally analogous proteins

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 sol...

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Detalles Bibliográficos
Autores principales: Kawale, Ashish A., Burmann, Björn M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8567434/
https://www.ncbi.nlm.nih.gov/pubmed/34761231
http://dx.doi.org/10.1016/j.xpro.2021.100919
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author Kawale, Ashish A.
Burmann, Björn M.
author_facet Kawale, Ashish A.
Burmann, Björn M.
author_sort Kawale, Ashish A.
collection PubMed
description 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).
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spelling pubmed-85674342021-11-09 Characterization of backbone dynamics using solution NMR spectroscopy to discern the functional plasticity of structurally analogous proteins Kawale, Ashish A. Burmann, Björn M. STAR Protoc Protocol 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). Elsevier 2021-10-29 /pmc/articles/PMC8567434/ /pubmed/34761231 http://dx.doi.org/10.1016/j.xpro.2021.100919 Text en © 2021 The Author(s) https://creativecommons.org/licenses/by/4.0/This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Protocol
Kawale, Ashish A.
Burmann, Björn M.
Characterization of backbone dynamics using solution NMR spectroscopy to discern the functional plasticity of structurally analogous proteins
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 Protocol
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8567434/
https://www.ncbi.nlm.nih.gov/pubmed/34761231
http://dx.doi.org/10.1016/j.xpro.2021.100919
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