Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.febslet.2011.08.048
Title: Selective and specific ion binding on proteins at physiologically-relevant concentrations
Authors: Miao, L.
Qin, H. 
Koehl, P.
Song, J. 
Keywords: Ephrin-B2
Hofmeister series
Insoluble protein
Intrinsically unstructured protein
NMR spectroscopy
Protein-ion interaction
Issue Date: 3-Oct-2011
Source: Miao, L., Qin, H., Koehl, P., Song, J. (2011-10-03). Selective and specific ion binding on proteins at physiologically-relevant concentrations. FEBS Letters 585 (19) : 3126-3132. ScholarBank@NUS Repository. https://doi.org/10.1016/j.febslet.2011.08.048
Abstract: Insoluble proteins dissolved in unsalted water appear to have no well-folded tertiary structures. This raises a fundamental question as to whether being unstructured is due to the absence of salt ions. To address this issue, we solubilized the insoluble ephrin-B2 cytoplasmic domain in unsalted water and first confirmed using NMR spectroscopy that it is only partially folded. Using NMR HSQC titrations with 14 different salts, we further demonstrate that the addition of salt triggers no significant folding of the protein within physiologically relevant ion concentrations. We reveal however that their 8 anions bind to the ephrin-B2 protein with high affinity and specificity at biologically-relevant concentrations. Interestingly, the binding is found to be both salt- and residue-specific. © 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Source Title: FEBS Letters
URI: http://scholarbank.nus.edu.sg/handle/10635/76927
ISSN: 00145793
DOI: 10.1016/j.febslet.2011.08.048
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