Hydrogen bonds are a primary driving force for de novo protein folding.

In this report, we demonstrate that (i) high pH values lead to the successful refolding of all protein candidates that we tested, (ii) secondary-structure formation is observable up to pH 12.0 by CD spectroscopy, (iii) partial native structure of a protein is detectable at pH 11.5–12.5 by SAXS and (iv) a positive trend towards main-chain polarization was observed as the pH increased to pH 12.0 by UVRR.

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