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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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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2023
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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 |
Sumario: | [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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