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Quantification of the Redox State of Protein Disulphide Bonds
1The Centenary Institute, NHMRC Clinical Trials Centre, Sydney Medical School, University of Sydney, Sydney, NSW, Australia. joyce.chiu@sydney.edu.au.
Abstract:
To elucidate how a functional disulphide bond controls protein activity, it is critical that the redox state of the bond in the population of protein molecules is known. A differential cysteine alkylation and mass spectrometry technique is described that affords precise quantification of protein disulphide bond redox state. The utility of the technique is demonstrated by quantifying the redox state of 31 of the 37 disulphide bonds in human αIIbβ3 integrin.
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When atoms gain or lose electrons to achieve a more stable electron configuration they form ions. Ionic bonds are electrostatic attractions between ions with opposite charges. Ionic compounds are rigid and brittle when solid and may dissociate into their constituent ions in water. Covalent compounds, by contrast, remain intact unless a chemical reaction breaks them.
Opposing Charges Hold Ions Together in Ionic Compounds
Ionic bonds are reversible electrostatic interactions between ions...

