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Cooperative Change in the Internal Dynamics of Streptavidin Caused by Biotin Binding

[Image: see text] Protein–ligand interactions are of vital importance for biological functions. The biological function of proteins, such as ligand-binding, is strongly influenced by their dynamics. Quasielastic neutron scattering (QENS) was used to investigate the internal molecular dynamics of str...

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Autor principal: Sarter, Mona
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2023
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10108356/
https://www.ncbi.nlm.nih.gov/pubmed/36988313
http://dx.doi.org/10.1021/acs.jpcb.3c00427
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author Sarter, Mona
author_facet Sarter, Mona
author_sort Sarter, Mona
collection PubMed
description [Image: see text] Protein–ligand interactions are of vital importance for biological functions. The biological function of proteins, such as ligand-binding, is strongly influenced by their dynamics. Quasielastic neutron scattering (QENS) was used to investigate the internal molecular dynamics of streptavidin (STV). QENS experiments to probe the internal dynamics were performed on a ps and 50–100 ps timescale using inverted geometry time-of-flight spectrometers. At the 50–100 ps timescale, the internal equilibrium motions of streptavidin proved to be unaffected by biotin (B) binding. However, on the ps timescale, suppression of jump-diffusion is observed even upon partial ligand saturation. This change indicates that the entire STV protein was affected by the population of one of the four binding sites, thus supporting a cooperative effect.
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spelling pubmed-101083562023-04-18 Cooperative Change in the Internal Dynamics of Streptavidin Caused by Biotin Binding Sarter, Mona J Phys Chem B [Image: see text] Protein–ligand interactions are of vital importance for biological functions. The biological function of proteins, such as ligand-binding, is strongly influenced by their dynamics. Quasielastic neutron scattering (QENS) was used to investigate the internal molecular dynamics of streptavidin (STV). QENS experiments to probe the internal dynamics were performed on a ps and 50–100 ps timescale using inverted geometry time-of-flight spectrometers. At the 50–100 ps timescale, the internal equilibrium motions of streptavidin proved to be unaffected by biotin (B) binding. However, on the ps timescale, suppression of jump-diffusion is observed even upon partial ligand saturation. This change indicates that the entire STV protein was affected by the population of one of the four binding sites, thus supporting a cooperative effect. American Chemical Society 2023-03-29 /pmc/articles/PMC10108356/ /pubmed/36988313 http://dx.doi.org/10.1021/acs.jpcb.3c00427 Text en © 2023 The Author. Published by American Chemical Society https://creativecommons.org/licenses/by/4.0/Permits the broadest form of re-use including for commercial purposes, provided that author attribution and integrity are maintained (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Sarter, Mona
Cooperative Change in the Internal Dynamics of Streptavidin Caused by Biotin Binding
title Cooperative Change in the Internal Dynamics of Streptavidin Caused by Biotin Binding
title_full Cooperative Change in the Internal Dynamics of Streptavidin Caused by Biotin Binding
title_fullStr Cooperative Change in the Internal Dynamics of Streptavidin Caused by Biotin Binding
title_full_unstemmed Cooperative Change in the Internal Dynamics of Streptavidin Caused by Biotin Binding
title_short Cooperative Change in the Internal Dynamics of Streptavidin Caused by Biotin Binding
title_sort cooperative change in the internal dynamics of streptavidin caused by biotin binding
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10108356/
https://www.ncbi.nlm.nih.gov/pubmed/36988313
http://dx.doi.org/10.1021/acs.jpcb.3c00427
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