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  Inclusion of ionization states of ligands in affinity calculations.

Donnini, S., Villa, A., Groenhof, G., Mark, A. E., Wierenga, R. K., & Juffer, A. H. (2009). Inclusion of ionization states of ligands in affinity calculations. Proteins: Structure, Function, and Bioinformatics, 76(1), 138-150. Retrieved from http://www3.interscience.wiley.com/cgi-bin/fulltext/121520147/PDFSTART.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0012-D80D-E Version Permalink: https://hdl.handle.net/11858/00-001M-0000-0027-EF57-8
Genre: Journal Article

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 Creators:
Donnini, S.1, Author           
Villa, A., Author
Groenhof, G.1, Author           
Mark, A. E., Author
Wierenga, R. K., Author
Juffer, A. H., Author
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1Department of Theoretical and Computational Biophysics, MPI for biophysical chemistry, Max Planck Society, ou_578631              

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Free keywords: binding free energy; effective affinity; molecular dynamics; pK calculations; protonation equilibria; thermodynamic integration; triosephosphate isomerase
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Language(s): eng - English
 Dates: 2009-07
 Publication Status: Issued
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 Identifiers: eDoc: 433092
URI: http://www3.interscience.wiley.com/cgi-bin/fulltext/121520147/PDFSTART
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Title: Proteins: Structure, Function, and Bioinformatics
Source Genre: Journal
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Pages: - Volume / Issue: 76 (1) Sequence Number: - Start / End Page: 138 - 150 Identifier: -