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|
| Type |
Poster Presentation |
| Area |
Physical Chemistry |
| Room No. |
Event Hall |
| Time |
4월 20일 (금요일) 11:00~12:30 |
| Code |
PHYS.P-106 |
| Subject |
Mechanism of fluorescence enhancement of a ligand-inducible fluorescent protein |
| Authors |
Euihyun Lee, Sang-Hee Shim, MINHAENG CHO*
Department of Chemistry, Korea University, Korea
|
| Abstract |
Recently, Yeh et al. reported a series of mutants of UnaG protein, a ligand-activated fluorescent protein in which the ligand (bilirubin) binds to the protein through noncovalent interaction. One of the mutants, named as eUnaG, has significantly higher fluorescence intensity and thermal stability than the wild type. Another mutant, named as V2P, has lower fluorescence intensity. Interestingly, the single mutation site is distant from the fluorophore, which renders the mechanism of such fluorescence enhancement or reduction unclear. Here, we performed extensive MD simulations for the original UnaG, eUnaG and V2P to find the reason of enhanced fluorescence intensity. Based on a relation between a rigidity of chromophore and quantum yield, we carried out a detailed analysis from MD trajectories, and found the enhanced rigidity of bilirubin in eUnaG. Furthermore, our results revealed a structural change in a wide range throughout the protein structure, not only in the vicinity of the mutated site, which leads to the conformational and rotational change of bilirubin. Our research is important in an aspect on the noncovalently binding fluorescent protein, which has additional rotational degrees of freedom of chromophore and clearly proves the relation between the chromophore and overall protein structure. Thus, this can provide a new insight for engineering new class of fluorescent protein. |
| E-mail |
euihyun7@korea.ac.kr |
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121st General Meeting of the KCS