Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2021414 | Protein Expression and Purification | 2009 | 4 Pages |
Abstract
In this study, we report the simultaneous refolding and reconstitution of the recombinant Bax inhibitor-1 (BI-1) from inclusion bodies expressed in Escherichia coli. A functional assay showed that the resulting proteoliposomes responded to acidic conditions and triggered the release of entrapped Ca2+ from liposomes. The secondary structure of the reconstituted BI-1 was also determined using circular dichroism, which revealed an increase of α-helix content and a decrease of random structure when exposed to acidic solutions. These conformational changes may be responsible for the proton ion-induced Ca2+ release of BI-1.
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Authors
Taeho Ahn, Chul-Ho Yun, Ho Zoon Chae, Hyung-Ryong Kim, Han-Jung Chae,