Selective and specific ion binding on proteins at physiologically-relevant concentrations.

摘要: Insoluble proteins dissolved in unsalted water appear to have no well-folded tertiary structures. This raises a fundamental question as whether being unstructured is due the absence of salt ions. To address this issue, we solubilized insoluble ephrin-B2 cytoplasmic domain and first confirmed using NMR spectroscopy that it only partially folded. Using HSQC titrations with 14 different salts, further demonstrate addition triggers significant folding protein within physiologically relevant ion concentrations. We reveal however their 8 anions bind high affinity specificity at biologically-relevant Interestingly, binding found be both salt- residue-specific.