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- W2983171608 abstract "Molecular dynamics plays an important role for the biological function of proteins. For protein ligand interactions, changes of conformational entropy of protein and hydration layer are relevant for the binding process. Quasielastic neutron scattering (QENS) was used to investigate differences in protein dynamics and conformational entropy of ligand-bound and ligand-free streptavidin. Protein dynamics were probed both on the fast picosecond time scale using neutron time-of-flight spectroscopy and on the slower nanosecond time scale using high-resolution neutron backscattering spectroscopy. We found the internal equilibrium motions of streptavidin and the corresponding mean square displacements (MSDs) to be greatly reduced upon biotin binding. On the basis of the observed MSDs, we calculated the difference of conformational entropy ΔSconf of the protein component between ligand-bound and ligand-free streptavidin. The rather large negative ΔSconf value (−2 kJ mol–1 K–1 on the nanosecond time scale) obtained for the streptavidin tetramer seems to be counterintuitive, given the exceptionally high affinity of streptavidin–biotin binding. Literature data on the total entropy change ΔS observed upon biotin binding to streptavidin, which includes contributions from both the protein and the hydration water, suggest partial compensation of the unfavorable ΔSconf by a large positive entropy gain of the surrounding hydration layer and water molecules that are displaced during ligand binding." @default.
- W2983171608 created "2019-11-22" @default.
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- W2983171608 date "2019-11-11" @default.
- W2983171608 modified "2023-09-27" @default.
- W2983171608 title "Strong Adverse Contribution of Conformational Dynamics to Streptavidin–Biotin Binding" @default.
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- W2983171608 doi "https://doi.org/10.1021/acs.jpcb.9b08467" @default.
- W2983171608 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31710813" @default.
- W2983171608 hasPublicationYear "2019" @default.
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