These questions cover some of the basic concepts Proteins. These are to help you

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These questions cover some of the basic concepts Proteins. These are to help you make sure you have caught some of the basic points of the lecture, so that you will be ready for class, work on interpret these techniques. You do not have to turn in your answers to of these questions, or ones very much like them, will be on the quiz you will take at the begineing of class on Sept. 21 presented in the lecture on chapter 3b: Woeking with where we will work on aoquiring deeper understanding of howw to use and these questions; however, a subsct 1. Different purification techniques sort proteins on the basis of different protein properties. Match each technique to the property (or properties) of the proteins it uses. Multiple techniques may rely on the same property. Technique Property A. Size exclusion chromatography B. SDS-PAGE Gel electrophoresis C. 2D gel electrophoresis D. Ion exchange chromatography E. Subcellular fractionation i. Location of the protein in the cell ii. Protein change / isoelectric point iii. Protein size (natively folded) iv. Protein size (denatured) 2. Fill in the blanks of the following sentence with the terms "increase" and "decrease "During protein purification, the percent recovery of the protein will typically cetained at each step, but the specific activity should 3. Fill in the blank: A low speed spin (1,000 X g) pellets while a and a medium speed spin (-15,000 X g) also pellets high speed spin (-100,000 X g) also pellets Fill in the blank: On a western blot, the protein present. On an SDS-PAGE gel, of a band represents the approximate 4. tein, while theo of a band represents the amount of that Larger proteins run faster than small ones, just like on a size exclusion column Larger proteins run faster than small ones, the opposite of on a size exclusion column Smaller proteins run faster than large ones, just like on a size exclusion column Smaller proteins run faster than large ones, the opposite of on a size exclusion column 5. a. b. c. d. 6. .The mass of a protein is most often measured in a. kilobasepairs, kb b. kilodaltons, kDa c. kilograms, kg d. kilopascals, kPa

Explanation / Answer

6. kiloDaltons,kDa this is the most common unit that is used to measure the mass of a protein.

5. In SDS Page, proteins are separated based on their size with the smallest proteins moving fastest where as in case of size exclusion chromatography, the larger size particles move fast as they travel in the spaces between the stationary phase as compared to small particles which tend to move through the stationary phase particles.

So the answer must be option d. smaller proteins run faster than larger ones, the opposite of size exclusion chromatography.

4. position, thickness

3. cells and nuclei, membrane organelles, macromolecules.

2. decrease, increase

during protein purfication, the ultimate aim is to obtain a protein sample with no impurities. In this process certain amount of protein is lost at every stage but the ultimate goal is to have maximum specific activity.

1. Size exclusion chromatography- protein size (natively folded)

SDS PAGE- protein size (denatured)

2D gel electrophoresis: charge of a protein/pI of protein

Ion exchange: charge of a protein/pI of protein

Subcellular fractionation: location of protein in the cell (because different cell organeeles based on their size will be centrifuged and separated and for analysing the desired protein it is important to know the location of the cell where protein is present. So as to obtain our desired fraction.

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