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  Binding affinities controlled by shifting conformational equilibria: Opportunities and limitations.

Michielssens, S., de Groot, B. L., & Grubmüller, H. (2015). Binding affinities controlled by shifting conformational equilibria: Opportunities and limitations. Biophysical Journal, 108(10), 2585-2590. doi:10.1016/j.bpj.2015.04.012.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-7959-E Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-CDDD-E
Genre: Journal Article

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2157457.pdf (Publisher version), 979KB
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 Creators:
Michielssens, S.1, Author              
de Groot, B. L.1, Author              
Grubmüller, H.2, Author              
Affiliations:
1Research Group of Computational Biomolecular Dynamics, MPI for Biophysical Chemistry, Max Planck Society, ou_578573              
2Department of Theoretical and Computational Biophysics, MPI for biophysical chemistry, Max Planck Society, ou_578631              

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 Abstract: Conformational selection is an established mechanism in molecular recognition. Despite its power to explain binding events, it is hardly used in protein/ligand design to modulate molecular recognition. Here, we explore the opportunities and limitations of design by conformational selection. Using appropriate thermodynamic cycles, our approach predicts the effects of a conformational shift on binding affinity and also allows one to disentangle the effects induced by a conformational shift from other effects influencing the binding affinity. The method is assessed and applied to explain the contribution of a conformational shift on the binding affinity of six ubiquitin mutants showing different conformational shifts in six different complexes.

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Language(s): eng - English
 Dates: 2015-05-19
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.bpj.2015.04.012
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Title: Biophysical Journal
Source Genre: Journal
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Pages: - Volume / Issue: 108 (10) Sequence Number: - Start / End Page: 2585 - 2590 Identifier: -