@article { ISI:000274825700004,
	title = {Titration\_DB: Storage and analysis of NMR-monitored protein pH titration curves},
	journal = {PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS},
	volume = {78},
	number = {4},
	year = {2010},
	month = {MAR},
	pages = {843-857},
	abstract = {NMR-monitored pH titration experiments are routinely used to measure site-specific protein pKa values. Accurate experimental pKa values are essential in dissecting enzyme catalysis, in studying the pH-dependence of protein stability and ligand binding, in benchmarking pKa 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 pKa 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 reinterpretation. 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.},
	issn = {0887-3585},
	doi = {10.1002/prot.22611},
	author = {Farrell, Damien and Miranda, Emanuel Sa and Webb, Helen and Georgi, Nikolaj and Crowley, Peter B. and McIntosh, Lawrence P. and Nielsen, Jens Erik}
}
