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- W2068153876 abstract "Abstract NMR‐monitored pH titration experiments are routinely used to measure site‐specific protein p K a values. Accurate experimental p K a values are essential in dissecting enzyme catalysis, in studying the pH‐dependence of protein stability and ligand binding, in benchmarking p K a prediction algorithms, and ultimately in understanding electrostatic effects in proteins. However, due to the complex ways in which pH‐dependent electrostatic and structural changes manifest themselves in NMR spectra, reported apparent p K a values are often dependent on the way that NMR pH‐titration curves are analyzed. It is therefore important to retain the raw NMR spectroscopic data to allow for documentation and possible re‐interpretation. We have constructed a database of primary NMR pH‐titration data, which is accessible via a web interface. Here, we report statistics of the database contents and analyze the data with a global perspective to provide guidelines on best practice for fitting NMR titration curves. Titration_DB is available at http://enzyme.ucd.ie/Titration_DB . Proteins 2010. © 2009 Wiley‐Liss, Inc." @default.
- W2068153876 created "2016-06-24" @default.
- W2068153876 creator A5020483276 @default.
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- W2068153876 creator A5055591879 @default.
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- W2068153876 creator A5075617803 @default.
- W2068153876 creator A5082362785 @default.
- W2068153876 creator A5084919791 @default.
- W2068153876 date "2009-11-06" @default.
- W2068153876 modified "2023-10-12" @default.
- W2068153876 title "Titration_DB: Storage and analysis of NMR-monitored protein pH titration curves" @default.
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