1- In a non-denaturing polyacrylamide gel electrophoresis, what would be the ord
ID: 207349 • Letter: 1
Question
1- In a non-denaturing polyacrylamide gel electrophoresis, what would be the order of resolution from top to 5.5pts the bottom of the gel, - polypeptide A in its tertiary configuration JMW 50 KD) 2 denatured polypeptide A, (MW SO KD) 3- denatured polypeptide B, (MW 180 KD) 4 denatured polypeptide C (MW 100 KD) a. 4,3,2,1 b. 3,4,1,2 2,1,3,4 d. 3,4,2,1 e. 1,3,42 2- In SDS-PAGE,ISDS polyacrylamide gel)j the proteins are compressed at the top of resolving gel because of a. The low concentration of stacking eel b. The net charge of glycine at 6.8 pH C. The anionic charge of proteins d. All of the above e. a and c 3- Proteins are usually separated using polyacrylamide gel rather than agarose because: a. False, small protein resolve better in agarose gel than poyacrylamide b. True, Polyacrylamide gel has pore size larger than the size of protein molecules c. True, Polyacrylamide gel has pore size similar to the size of protein molecules d. False, agarose is a universal gel for resolution of small size molecules 4- SDS-PAGE,(SDS polyacrylamide gel) is used to: a. b. c. d. Detect the numbers of proteins in a sample Determine the molecular weight of proteins of interest Compare the proteins profiles of different species All of the above 5- The movement of a charged molecule subjected to an electrical field directly depends on a. The net charge of the molecule b. The frictional coefficient, mass and shape of the molecule c. The voltage of electric field d. All of the above e. a and c 6- There are two layers of gels in a discontinuous gel electrophoresis method which are characterized as a. The upper layer, a high concentration gel with pH of 6.8 gel b. The lower layer, a low concentration gel with pH of 8.8 c. The upper layer, a low concentration gel with pH of 8.8 d. The upper layer, a low concentration gel with pH of 6.8Explanation / Answer
1. The correct answer is option e) 1,3,4,2.
A polypeptide in tertiary configuration moves slower than a denatured polypeptide. A polypeptide in tertiary configuration is more compact and would have a larger surface area and therefore face more resistance in order to move through the pores as compared to the denatured form of the same polypeptide. Denatured polypeptides are basically linear therefore they face less resistance and can easily pass through the pores of the gel. High molecular weight polypeptides move more slowly through the gel than lower molecular weight polypeptides.
2. The correct answer is option e) a and c
In SDS-PAGE, there are two layers of gel. The top layer is called stacking gel and the bottom layer is called resolving gel. The stacking gel has large sized pores that concentrate all the proteins in one band at the top of the resolving gel so that they will start migrating at the same time and get resolved. This happened due to the low concentration of polyacrylamide in the gel and anionic charge of proteins. Then, the running gel separates the proteins based on their molecular weight.
3. The correct answer is option c) true, polyacrylamide gel has pore size similar to the size of protein molecules
4. The correct answer is option d) all of the above.
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