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. Folding of the four domains and dimerization are impaired by the G/y446-Glu exchange in human glutathione reductase
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. Extensive studies relating to the mechanism of glycosylation and its role in protein folding, stability, and function have been carried out by researchers in the field (7-9)
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. Purified proteins were dissolved in 8 M Urea and refolded by dialysis as described in Gursky and Atkinson (1996)
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. The AFM image of the fibroid of the total length of 544 ± 12 nm may be interpreted as either a periodically twisted structure with a regular helical thread of 52 ± 2 nm, or linearly-staggered elements, each 52 ± 2 nm long, constituting a longer topological block
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