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

ABSTRACT: The protein-folding mechanism remains a major puzzle in life science. Purified soluble activation-induced cytidine deaminase (AID) is one of the most difficult proteins to obtain. Starting from inclusion bodies containing a C-terminally truncated version of AID (residues 1-153; AID¹⁵³), an optimized in vitro folding procedure was derived to obtain large amounts of AID¹⁵³, which led to crystals with good quality and to final structural determination. Interestingly, it was found that the final refolding yield of the protein is proline residue-dependent. The difference in the distribution of cis and trans configurations of proline residues in the protein after complete denaturation is a major determining factor of the final yield. A point mutation of one of four proline

SUBMITTER: Lee S 

PROVIDER: S-EPMC5713874 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature