MTGFP融合蛋白摺疊過程中分子內螢光能量轉移研究

姜芳馨

doi:10.6842/NCTU.2009.00652

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MTGFP融合蛋白摺疊過程中分子內螢光能量轉移研究

Intramolecular Fluorescence Energy Transfer Study of MTGFP fusion protein during protein folding process

姜芳馨 , Masters　　Advisor：張家靖　　

繁體中文 DOI： 10.6842/NCTU.2009.00652

金屬硫蛋白； HASH(0xaad9a20) ；綠色螢光蛋白； Metallothionein ； HASH(0xaad9f6c) ； Green Fluorescence Protein

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Protein folding status indicator is highly desired for revealing the folding process in real time. Therefore, ultra sensitive detection system in molecular scale is required. In this study, we designed an intramolecular fluorescence resonance energy transfer (FRET) system to monitor the folding status of metal binding protein, metallothionein (MT) by liking with green fluorescence protein (GFP). Both FRET and quench effect took place when the protein folding followed the over-critical reaction path. This new perspectives may provide significant strategy for investigation of protein folding process in real time.Metallothionein (MT) is a 61 amino-acids protein which contains 20 cysteine residues and forms two metal binding clusters (α-, β-domains). Green fluorescent protein (GFP), which emits green fluorescent light (λ max = 508 nm) by exciting with ultraviolet light (395 nm), can be used as a fluorophore in fluorescence resonance energy transfer (FRET) system. A fusion protein of MTGFP was cloned and refolded to native form by stepwise thermal equilibrium dialysis (TED). Both dynamic light scattering (DLS) and circular dichroism (CD) spectra indicate that the fusion protein has been refolded to its native state. The inductively couple plasma-mass (ICP-mass) spectrum also indicates that the refolded-MTGFP has restored its metal binding capability However, the fluorescence intensity of MTGFP at 508 nm declines during the refolding process. Therefore the MT seems acting as a quencher of GFP when it folds to native state. Namely, there is intramolecular fluorescence energy transfer taking place between MT and GFP. This new perspectives may provide significant strategy for investigation of protein folding process.

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