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How to distinguish conformational selection and induced fit based on chemical relaxation rates

MPS-Authors
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Paul,  Fabian
Thomas Weikl, Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Weikl,  Thomas R.
Thomas Weikl, Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Citation

Paul, F., & Weikl, T. R. (2016). How to distinguish conformational selection and induced fit based on chemical relaxation rates. PLoS Computational Biology, 12(9): e1005067. doi:10.1371/journal.pcbi.1005067.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002B-602A-6
Abstract
Protein binding often involves conformational changes. Important questions are whether a conformational change occurs prior to a binding event (‘conformational selection’) or after a binding event (‘induced fit’), and how conformational transition rates can be obtained from experiments. In this article, we present general results for the chemical relaxation rates of conformational-selection and induced-fit binding processes that hold for all concentrations of proteins and ligands and, thus, go beyond the standard pseudo-first-order approximation of large ligand concentration. These results allow to distinguish conformational-selection from induced-fit processes—also in cases in which such a distinction is not possible under pseudo-first-order conditions—and to extract conformational transition rates of proteins from chemical relaxation data.