Site-directed fluorescence approaches to monitor the structural dynamics of proteins using intrinsic Trp and labeled with extrinsic fluorophores

Comprehensive understanding of a protein’s function depends on having reliable, sophisticated tools to study protein structural dynamics in physiologically-relevant conditions. Here, we present an effective, robust step-by-step protocol to monitor the structural dynamics (including hydration dynamic...

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Detalles Bibliográficos
Autores principales: Brahma, Rupasree, Das, Anindita, Raghuraman, H.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2022
Materias:
Protocol
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8889417/
https://www.ncbi.nlm.nih.gov/pubmed/35252885
http://dx.doi.org/10.1016/j.xpro.2022.101200
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author Brahma, Rupasree
Das, Anindita
Raghuraman, H.
author_facet Brahma, Rupasree
Das, Anindita
Raghuraman, H.
author_sort Brahma, Rupasree
collection PubMed
description Comprehensive understanding of a protein’s function depends on having reliable, sophisticated tools to study protein structural dynamics in physiologically-relevant conditions. Here, we present an effective, robust step-by-step protocol to monitor the structural dynamics (including hydration dynamics) of a protein utilizing various site-directed fluorescence (SDFL) approaches. This protocol should be widely applicable for studying soluble proteins, intrinsically-disordered proteins, and membrane proteins. For complete details on the use and execution of this protocol, please refer to Das et al. (2020), Das and Raghuraman (2021), and Chatterjee et al. (2021).
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spelling pubmed-88894172022-03-03 Site-directed fluorescence approaches to monitor the structural dynamics of proteins using intrinsic Trp and labeled with extrinsic fluorophores Brahma, Rupasree Das, Anindita Raghuraman, H. STAR Protoc Protocol Comprehensive understanding of a protein’s function depends on having reliable, sophisticated tools to study protein structural dynamics in physiologically-relevant conditions. Here, we present an effective, robust step-by-step protocol to monitor the structural dynamics (including hydration dynamics) of a protein utilizing various site-directed fluorescence (SDFL) approaches. This protocol should be widely applicable for studying soluble proteins, intrinsically-disordered proteins, and membrane proteins. For complete details on the use and execution of this protocol, please refer to Das et al. (2020), Das and Raghuraman (2021), and Chatterjee et al. (2021). Elsevier 2022-02-28 /pmc/articles/PMC8889417/ /pubmed/35252885 http://dx.doi.org/10.1016/j.xpro.2022.101200 Text en © 2022 The Author(s) https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Protocol
Brahma, Rupasree
Das, Anindita
Raghuraman, H.
Site-directed fluorescence approaches to monitor the structural dynamics of proteins using intrinsic Trp and labeled with extrinsic fluorophores
title Site-directed fluorescence approaches to monitor the structural dynamics of proteins using intrinsic Trp and labeled with extrinsic fluorophores
title_full Site-directed fluorescence approaches to monitor the structural dynamics of proteins using intrinsic Trp and labeled with extrinsic fluorophores
title_fullStr Site-directed fluorescence approaches to monitor the structural dynamics of proteins using intrinsic Trp and labeled with extrinsic fluorophores
title_full_unstemmed Site-directed fluorescence approaches to monitor the structural dynamics of proteins using intrinsic Trp and labeled with extrinsic fluorophores
title_short Site-directed fluorescence approaches to monitor the structural dynamics of proteins using intrinsic Trp and labeled with extrinsic fluorophores
title_sort site-directed fluorescence approaches to monitor the structural dynamics of proteins using intrinsic trp and labeled with extrinsic fluorophores
topic Protocol
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8889417/
https://www.ncbi.nlm.nih.gov/pubmed/35252885
http://dx.doi.org/10.1016/j.xpro.2022.101200
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