Unfolding and Refolding of Disulfide Proteins Using the Method Disulfide Scrambling
Author:
Chang Rowen J. Y.
Publisher
Springer New York
Reference67 articles.
1. Antuch W, Güntert P, Billeter M, Hawthorne T, Grossenbacher H, Wüthrich K (1994) NMR solution structure of recombinant tick anticoagulant protein (rTAP), a factor Xa inhibitor from the tick Ornithodoros moubata. FEBS Lett 352:251–257
2. Arolas JL, Aviles FX, Chang J-Y, Ventura S (2006) Folding of small disulfide-rich proteins: clarifying the puzzle. Trends Biochem Sci 31:292–301
3. Arias-Moreno X, Arolas JL, Aviles FX, Sancho J, Ventura S (2008) Scrambled isomers as key intermediates in the oxidative folding of liogand binding module 5 of the low density lipoprotein receptor. J Biol Chem 283:13627–13637
4. Arolas JL, Sanglas L, Lorenzo J, Bronsoms S, Aviles FX (2009) Insights into the two-domain architecture of the metallocarboxypeptidase inhibitor from the Ascaris parasite inferred from the mechanism of its oxidative folding. Biochemistry 48:8225–8232
5. Cemazar M, Zahariev S, Lopez JJ, Carugo O, Jones JA, Hore PJ, Pongor S (2003) Oxidative folding intermediates with nonnative disulfide bridges between adjacent cysteine residues. Proc Natl Acad Sci USA 100:5754–5759