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| Type |
Poster Presentation |
| Area |
생명화학 |
| Room No. |
포스터발표장 |
| Time |
4월 21일 (금요일) 13:00~14:30 |
| Code |
BIO.P-313 |
| Subject |
Expression, purification and functionality of soluble ERLBD domain |
| Authors |
윤소영*, 이경희
세종대학교 화학과, Korea
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| Abstract |
Discovery of destabilization domains (DDs) of estrogen receptor ligand binding domain(ERLBD, 297-549) have led us to investigate the regulatory role of these domains on fibril formation of amyloidogenic proteins, such as α-Synuclein (αSyn) as well as human islet amyloid polypeptide (hIAPP). For the purpose of overexpression and purification of soluble ERLBD, we have constructed the original plasmid ERLBD297-549/ pET28a. Upon induction by IPTG, ERLBD was overexpressed in bacteria, but purification was not successful because of insolubility. Here, we compare the other domain construct (ERLBD302-552) with ERLBD297-549 in order to search for the optimized condition of purification. Functional role of ERLBD302-552 on amyloid fibril formation is also discussed based on Thioflavin T (ThT) fluorescence.
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| E-mail |
gee0528@gmail.com |
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119th General Meeting of the KCS