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. Thermal denaturation of rSBA and gSBA Thermal unfolding profiles of both nonglycosylated and glycosylated SBA were monitored by the change in molar ellipticity value at 218 nm at a protein concentration of 13 µM
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. Using these procedures, the energetics and pathways of folding, as well as the existence of transient intermediate states between unfolded and fully folded polypeptides, have been characterized for a number of proteins (for a collection of reviews, see Creighton, 1992; Pain, 1994)
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