Function-Related Dynamics in Multi-Spanning Helical Membrane Proteins Revealed by Solution NMR

A primary biological function of multi-spanning membrane proteins is to transfer information and/or materials through a membrane by changing their conformations. Therefore, particular dynamics of the membrane proteins are tightly associated with their function. The semi-atomic resolution dynamics in...

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Detalles Bibliográficos
Autores principales: Takeuchi, Koh, Kofuku, Yutaka, Imai, Shunsuke, Ueda, Takumi, Tokunaga, Yuji, Toyama, Yuki, Shiraishi, Yutaro, Shimada, Ichio
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Review
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8398610/
https://www.ncbi.nlm.nih.gov/pubmed/34436367
http://dx.doi.org/10.3390/membranes11080604
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author Takeuchi, Koh
Kofuku, Yutaka
Imai, Shunsuke
Ueda, Takumi
Tokunaga, Yuji
Toyama, Yuki
Shiraishi, Yutaro
Shimada, Ichio
author_facet Takeuchi, Koh
Kofuku, Yutaka
Imai, Shunsuke
Ueda, Takumi
Tokunaga, Yuji
Toyama, Yuki
Shiraishi, Yutaro
Shimada, Ichio
author_sort Takeuchi, Koh
collection PubMed
description A primary biological function of multi-spanning membrane proteins is to transfer information and/or materials through a membrane by changing their conformations. Therefore, particular dynamics of the membrane proteins are tightly associated with their function. The semi-atomic resolution dynamics information revealed by NMR is able to discriminate function-related dynamics from random fluctuations. This review will discuss several studies in which quantitative dynamics information by solution NMR has contributed to revealing the structural basis of the function of multi-spanning membrane proteins, such as ion channels, GPCRs, and transporters.
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spelling pubmed-83986102021-08-29 Function-Related Dynamics in Multi-Spanning Helical Membrane Proteins Revealed by Solution NMR Takeuchi, Koh Kofuku, Yutaka Imai, Shunsuke Ueda, Takumi Tokunaga, Yuji Toyama, Yuki Shiraishi, Yutaro Shimada, Ichio Membranes (Basel) Review A primary biological function of multi-spanning membrane proteins is to transfer information and/or materials through a membrane by changing their conformations. Therefore, particular dynamics of the membrane proteins are tightly associated with their function. The semi-atomic resolution dynamics information revealed by NMR is able to discriminate function-related dynamics from random fluctuations. This review will discuss several studies in which quantitative dynamics information by solution NMR has contributed to revealing the structural basis of the function of multi-spanning membrane proteins, such as ion channels, GPCRs, and transporters. MDPI 2021-08-09 /pmc/articles/PMC8398610/ /pubmed/34436367 http://dx.doi.org/10.3390/membranes11080604 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Takeuchi, Koh
Kofuku, Yutaka
Imai, Shunsuke
Ueda, Takumi
Tokunaga, Yuji
Toyama, Yuki
Shiraishi, Yutaro
Shimada, Ichio
Function-Related Dynamics in Multi-Spanning Helical Membrane Proteins Revealed by Solution NMR
title Function-Related Dynamics in Multi-Spanning Helical Membrane Proteins Revealed by Solution NMR
title_full Function-Related Dynamics in Multi-Spanning Helical Membrane Proteins Revealed by Solution NMR
title_fullStr Function-Related Dynamics in Multi-Spanning Helical Membrane Proteins Revealed by Solution NMR
title_full_unstemmed Function-Related Dynamics in Multi-Spanning Helical Membrane Proteins Revealed by Solution NMR
title_short Function-Related Dynamics in Multi-Spanning Helical Membrane Proteins Revealed by Solution NMR
title_sort function-related dynamics in multi-spanning helical membrane proteins revealed by solution nmr
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8398610/
https://www.ncbi.nlm.nih.gov/pubmed/34436367
http://dx.doi.org/10.3390/membranes11080604
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