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  Accurate and rigorous prediction of the changes in protein free energies in a large-scale mutation scan.

Gapsys, V., Michielssens, S., Seeliger, D., & de Groot, B. L. (2016). Accurate and rigorous prediction of the changes in protein free energies in a large-scale mutation scan. Angewandte Chemie-International Edition, 55(26), 7364-7368. doi:10.1002/anie.201510054.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-EF25-F Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-EF29-7
Genre: Journal Article

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Gapsys, V.1, Author              
Michielssens, S.1, Author              
Seeliger, D.1, Author              
de Groot, B. L.1, Author              
Affiliations:
1Research Group of Computational Biomolecular Dynamics, MPI for biophysical chemistry, Max Planck Society, ou_578573              

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Free keywords: force field; free-energy calculations; proteins; thermostability
 Abstract: The prediction of mutation-induced free-energy changes in protein thermostability or protein–protein binding is of particular interest in the fields of protein design, biotechnology, and bioengineering. Herein, we achieve remarkable accuracy in a scan of 762 mutations estimating changes in protein thermostability based on the first principles of statistical mechanics. The remaining error in the free-energy estimates appears to be due to three sources in approximately equal parts, namely sampling, force-field inaccuracies, and experimental uncertainty. We propose a consensus force-field approach, which, together with an increased sampling time, leads to a free-energy prediction accuracy that matches those reached in experiments. This versatile approach enables accurate free-energy estimates for diverse proteins, including the prediction of changes in the melting temperature of the membrane protein neurotensin receptor 1.

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Language(s): eng - English
 Dates: 2016-04-282016-06-20
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1002/anie.201510054
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Title: Angewandte Chemie-International Edition
Source Genre: Journal
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Pages: - Volume / Issue: 55 (26) Sequence Number: - Start / End Page: 7364 - 7368 Identifier: -