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

• DOI: 10.1021/acs.jpcb.3c00427
• Publication Date: 2023-03-29T18:32:45Z
• Authors: Mona Sarter
• Keywords: Streptavidin; Protein Dynamics; Dynamics; Quasielastic neutron scattering

Protein-ligand interactions are of vital importance for biological functions. The function proteins, such as ligand-binding, is strongly influenced by their dynamics. Quasielastic neutron scattering (QENS) was used to investigate the internal molecular dynamics streptavidin (STV). QENS experiments probe were performed on a ps and 50-100 timescale using inverted geometry time-of-flight spectrometers. At timescale, equilibrium motions proved be unaffected biotin (B) binding. However, suppression jump-diffusion observed even upon partial ligand saturation. This change indicates that entire STV protein affected population one four binding sites, thus supporting cooperative effect.