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![[Figure 4]](qh5051fig4mag.jpg)
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Figure 4
(a) Size-exclusion chromatography assay of RuBisCo refolded at various pH values. When refolded at pH 7.5, RuBisCo predominantly formed misfolded aggregates that eluted at the void volume. As the refolding pH increased to 11.5, the resultant eluate better resembled the native protein. (b) Refolded DapA can be crystallized under the same conditions as used for native DapA. This demonstrates that the refolded protein has the same properties as the native protein. (c) Kratky plots of SAXS results for DapA refolding under different pH conditions. Three-dimensional structures of DapA were observed to begin formation at pH 12.5. (d) 4 h protein refolding procedure: the percentage of refolded protein concentration recovered relative to the 9 M urea-solubilized unfolded protein concentration. Upon complete denaturation via boiling, mAID153, which contains a point mutation at Pro72, led to the recovery of ∼68% more refolded protein compared with AID153. |
![[Figure 4]](qh5051fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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