Cargando…
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...
Autores principales: | , |
---|---|
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 |
_version_ | 1784594231370711040 |
---|---|
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). |
format | Online Article Text |
id | pubmed-8567434 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT kawaleashisha characterizationofbackbonedynamicsusingsolutionnmrspectroscopytodiscernthefunctionalplasticityofstructurallyanalogousproteins AT burmannbjornm characterizationofbackbonedynamicsusingsolutionnmrspectroscopytodiscernthefunctionalplasticityofstructurallyanalogousproteins |