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  How to Distinguish Conformational Selection and Induced Fit Based on Chemical Relaxation Rates

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-602A-6 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-67E6-6
Genre: Journal Article

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 Creators:
Paul, Fabian1, Author              
Weikl, Thomas R.1, Author              
Affiliations:
1Thomas Weikl, Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863330              

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Free keywords: Open Access
 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.

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 Dates: 2016-09-162016
 Publication Status: Published in print
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 Rev. Type: -
 Identifiers: DOI: 10.1371/journal.pcbi.1005067
BibTex Citekey: 10.1371/journal.pcbi.1005067
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Title: PLoS Computational Biology
Source Genre: Journal
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Publ. Info: San Francisco, CA : Public Library of Science
Pages: - Volume / Issue: 12 (9) Sequence Number: e1005067 Start / End Page: - Identifier: ISSN: 1553-734X