ArticleThe journal of physical chemistry. B2023
Cooperative Change in the Internal Dynamics of Streptavidin Caused by Biotin Binding.
Article in The journal of physical chemistry. B, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 5 citations in OpenAlex.
- Data Analysis of Dynamics in Protein Solutions Using Quasi-Elastic Neutron Scattering─Important Insights from Polarized Neutrons.Journal of the American Chemical Society · 2024Article
- Molecular Modeling, Synthesis, and Antihyperglycemic Activity of the New Benzimidazole Derivatives - Imidazoline Receptor Agonists.Drug design, development and therapy · 2024Article
- Avidin cooperative allosterism upon binding biotin observed by differential changes in intrinsic fluorescence.Biochemistry and biophysics reports · 2023Article
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Authors and funding
1 author at 1 institution in 1 country.
Funding
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Abstract
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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Registered trials
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