Thread: Coupled effect of salt and ph on proteins probed with NMR spectroscopy
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Unread 06-27-2013, 02:10 PM
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Default Coupled effect of salt and ph on proteins probed with NMR spectroscopy
Coupled effect of salt and ph on proteins probed with NMR spectroscopy

Publication date: Available online 27 June 2013
Source:Chemical Physics Letters

Author(s): Predrag Kukic , Fergal O’Meara , Chandralal Hewage , Jens ErikNielsen

The coupled effect of ionic strength (50-400mM) and pH (2-8) on ionization and conformation equilibria of lysozyme was studied using NMR spectroscopy. Observed changes in pKa values of the ionizable groups were found to originate from perturbations in the geometry of hydrogen bonds rather than screening of electric fields. Moreover, at the ionic strengths used here, salt-induced local conformational changes had a dominant effect on chemical shifts measured on 1HN and 15N amide nuclei. Accurate modelling of these localized perturbations in structure-based energy calculations is a necessary prerequisite on the way to complete understanding of any salt-induced processes in proteins.
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