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− | Amyloid-Beta and Tau are proteins which are known to be linked to the development of Alzheimer's disease, though the cause of the disease is still unknown [1]. They are both found in the brain in and around our neurons, and during Alzheimer's disease they accumulate to form plaques and tangles [2, 3]. The study of these aggregates are often done by staining them(4), which in turn demands an amount of the plaques great enough for staining. To instead study the early development of the aggregates a new method has to be developed. This could be studied by fusing a fluorescent markers like Green Fluorescent Protein (GFP) with the aggregation prone proteins. The problem is that when these marker are combined with the aggregation prone protein they become hard to express in Escherichia coli [5]. Therefore this year’s project is to optimize the expression the fusion proteins containing a fluorescent marker and amyloid-beta or tau in E. Coli. | + | Amyloid-Beta and Tau are proteins which are known to be linked to the development of Alzheimer's disease, though the cause of the disease is still unknown [1]. They are both found in the brain in and around our neurons, and during Alzheimer's disease they accumulate to form plaques and tangles [2, 3]. The study of these aggregates are often done by staining them(4), which in turn demands an amount of the plaques great enough for staining. To instead study the early development of the aggregates a new method has to be developed. This could be studied by fusing a fluorescent markers like Green Fluorescent Protein (GFP) with the aggregation prone proteins. The problem is that when these marker are combined with the aggregation prone protein they become hard to express in Escherichia coli [5]. <u>Therefore this year’s project is to optimize the expression the fusion proteins containing a fluorescent marker and amyloid-beta or tau in E. Coli. </u> |
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To optimize the expression of the proteins we will be using overexpressed chaperones. Chaperones are proteins that can help other proteins to fold into their native three-dimensional shape, for example by dissolving aggregates and guiding both unfolded and misfolded proteins to their correctly folded form [6]. During our project we will be using four different chaperones and we will see how different combinations of these affect the expression of Amyloid-beta and Tau respectively. | To optimize the expression of the proteins we will be using overexpressed chaperones. Chaperones are proteins that can help other proteins to fold into their native three-dimensional shape, for example by dissolving aggregates and guiding both unfolded and misfolded proteins to their correctly folded form [6]. During our project we will be using four different chaperones and we will see how different combinations of these affect the expression of Amyloid-beta and Tau respectively. |
Revision as of 11:50, 28 October 2017