Folding and unfolding mechanism of highly stable full-consensus ankyrin repeat proteins.

Abstract

Full-consensus designed ankyrin repeat proteins were designed with one to six identical repeats flanked by capping repeats. These proteins express well in Escherichia coli as soluble monomers. Compared to our previously described designed ankyrin repeat protein library, randomized positions have now been fixed according to sequence statistics and structural… (More)
DOI: 10.1016/j.jmb.2007.11.046

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