Strong Adverse Contribution of Conformational Dynamics to Streptavidin–Biotin Binding

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 pr...

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Veröffentlicht in:	The journal of physical chemistry. B 2020-01, Vol.124 (2), p.324-335
Hauptverfasser:	Sarter, Mona, Niether, Doreen, Koenig, Bernd W, Lohstroh, Wiebke, Zamponi, Michaela, Jalarvo, Niina H, Wiegand, Simone, Fitter, Jörg, Stadler, Andreas M
Format:	Artikel
Sprache:	eng
Schlagworte:	Bacterial Proteins - chemistry Bacterial Proteins - metabolism Binding Sites Biotin - chemistry Biotin - metabolism Diffusion Entropy Ligands Protein Binding Protein Conformation Streptavidin - chemistry Streptavidin - metabolism Streptomyces - chemistry Thermodynamics Water - chemistry Water - metabolism
Online-Zugang:	Volltext
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