Abstract
trans-3,4-Dihydroxyselenolane oxide (DHSox), a water-soluble cyclic selenoxide reagent, is useful for rapid and quantitative formation of disulphide (SS) bonds in a reduced state of SS-containing proteins because the selenoxide is a strong but selective oxidant for thiol substrates (RSH) in a wide range of pH. Due to this advantage over common disulphide reagents, such as oxidized dithiothreitol (DTTox) and glutathione (GSSG), DHSox enables clear characterization of oxidative folding pathways of proteins. DHSox is also useful for facile diagnosis of weakly folded structure, or reactivity (i.e., pKa) of the thiols, present in a reduced polypeptide chain and the partially oxidized folding intermediates, identification of the key SS intermediates that can be oxidized directly to the native state, and preparation of SS-scrambled misfolded protein species. In this chapter, these diverse utilities of DHSox in protein folding study are demonstrated.
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