Synonyms
Definition
Dynamic docking (DD) denotes a complex formed between reactive (electron transfer (ET)-active) protein partners in which a large ensemble of weakly-bound configurations of the complex contribute to binding, but only a few are reactive. Typically, the ET reaction occurs within the “thermodynamic” or “fast exchange” limit, in which case binding is effectively decoupled from reactivity, and it is possible to modulate reactivity without changing affinity.
Basic Characteristics
The DD Energy Landscape
Heterogeneity in the structure and dynamics of a macromolecule, and likewise of a complex between two macromolecules, is commonly visualized with an idealized “energy landscape,” an energy surface that represents the accessible configurations of the system on a hierarchy of energy/length scales (Wales 2004; Ubbink 2009). It has become increasingly clear that electron transfer protein partners commonly form complexes with dynamic structures, and are...
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References
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© 2013 European Biophysical Societies' Association (EBSA)
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Nocek, J.M., Hoffman, B.M. (2013). Dynamic Docking. In: Roberts, G.C.K. (eds) Encyclopedia of Biophysics. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-16712-6_17
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DOI: https://doi.org/10.1007/978-3-642-16712-6_17
Publisher Name: Springer, Berlin, Heidelberg
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