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

Lee, S.; Wang, C.; Liu, H.; Xiong, J.; Jiji, R.; Hong, X.; Yan, X.; Chen, Z.; Hammel, M.; Wang, Y.; Dai, S.; Wang, J.; Jiang, C.; Zhang, G.

doi:10.1107/S2059798317015303

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 3
(a) Location of prolines in AID¹⁵³. Pro72 was chosen as a site for point mutation to investigate the effects of proline in protein refolding. (b) 36–44 h protein-refolding procedure: the percentage of refolded protein concentration recovered relative to the 9 M urea-solubilized unfolded protein concentration. Subsequent runs of refolding and purifying AID¹⁵³ from the Ni–NTA flowthrough results in decreased recovery. Upon complete denaturation via boiling, mAID¹⁵³, which contains a point mutation at Pro72, led to the recovery of ∼91% more refolded protein compared with AID¹⁵³.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 73| Part 12| December 2017| Pages 955-969

https://doi.org/10.1107/S2059798317015303

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