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Independent Component 1 Approval
- In the process of protein crystallization first you have to purify the protein. Then you need to bring the protein/solution to a supersaturated state. Protein solubility is dependent on many factors which include the concentration and type of salt in the buffer, the pH of the buffer, and also the presence of possible co-factors. The most common way to reduce solubility is to add an "precipitant" which binds water molecules together and lowers water availability therefore making the concentration of protein higher, we will keep adding precipitants until we get the concentration we want. To get the crystallization to work you have to have the right solubility and this can get tricky, so for this process we are going to try different variations like a change in the pH or concentration until we get the protein to crystallize. After we get it crystallized we are going to use crystallography which is when we shoot a monochromatic(single wavelength) X-ray beam. It is continuously exposed to the beam while the crystal is rotating one degree, it then creates an image and the marks represent each diffraction that is reflected by the crystal.
- To show evidence of 30 hours of work I will document each variation combination that I did, make a lab report on the whole thing, and keep a log.
- This will help us better understand the enzyme (protein) that we are using in the process of creating renewable energy.
APPROVED
ReplyDeleteIn the process of protein crystallization first you have to purify the protein. Then you need to bring the protein/solution to a supersaturated state. Protein solubility is dependent on many factors which include the concentration and type of salt in the buffer, the pH of the buffer, and also the presence of possible co-factors. The most common way to reduce solubility is to add an "precipitant" which binds water molecules together and lowers water availability therefore making the concentration of protein higher, we will keep adding precipitants until we get the concentration we want. To get the crystallization to work you have to have the right solubility and this can get tricky, so for this process we are going to try different variations like a change in the pH or concentration until we get the protein to crystallize. After we get it crystallized we are going to use crystallography which is when we shoot a monochromatic(single wavelength) X-ray beam. It is continuously exposed to the beam while the crystal is rotating one degree, it then creates an image and the marks represent each diffraction that is reflected by the crystal.
To show evidence of 30 hours of work I will document each variation combination that I did, make a lab report on the whole thing, and keep a log.
This will help us better understand the enzyme (protein) that we are using in the process of creating renewable energy.