Homework Answers
Answer:
Protein B is larger than protein A because it has travelled less from the positive to negative end. Protein B is more positively charged than Protein A. So (a) is the correct answer.
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Based on the migration of proteins A, B, and C in these gels, which of the...
Based on the migration of proteins A, B, and C in these gels, which of the...
Based on the migration of proteins A, B, and C in these gels, which of the following statements is correct? Cathode (-) Anode (+) Native SDS-PAGE Select one a. Protein B is larger and more positively charged than Protein A b. Protein C is smaller and more positively charged than protein B c. Protein A is a small protein with a high positive charge d. Protein A is a large protein with a low positive charge Your answer is incorrect.
Based on the migration of 3 DNA fragments {A, B, & C) of the indicated sizes...
Based on the migration of 3 DNA fragments {A, B, & C) of the indicated sizes (where kb = kilobases, ie thousand base pairs) in these gels, which of the following statements is correct? А В С А В С kb 0.5 Gel #1 Gel #2 Select one: a. Gell #1 has a higher % agarose than gel #2 b. An 8% acrylamide gel would give greater resolution of fragments larger than 500 bp than either of these gels. c....
1. Which is a correct description of the use of separation techniques to separate a dipeptide...
1. Which is a correct description of the use of separation techniques to separate a dipeptide from a pentapeptide? a. the dipeptide emerges faster than the pentapeptide from a gel filtration column b. the dipeptide migrates faster towards the cathode than the pentapeptide on SDS-PAGE c. the dipeptide migrates to a more anodal position than the pentapeptide on electrofocusing d. the dipeptide sediments faster than the pentapeptide in an ultracentrifugal field e. none of these methods would separate the dipeptide...
I am confused on this question, the correct answer is A and I chose B. I...
I am confused on this question, the correct answer is A and I
chose B. I thought the cathode was positively charged, and the
anode was negateively charged; and a high PI would incicate a more
positive charge, and a low PI would incidate a more negative chare.
Are these correct or am I backwards in some these? Also, are any of
these different for a galvanic or electrolytic cell?
Please explain how you would answer this question, thank
you!...
14. Recombinant MBP-, GST- or GFP- fusion proteins are expressed in bacteria not only for affinity...
14. Recombinant MBP-, GST- or GFP- fusion proteins are expressed in bacteria not only for affinity chromatography but also to ___________. A. overexpress the proteins in bacteria B. to reduce toxicity of the foreign proteins C. for proper folding and keeping the proteins soluble D. to trace the cytological location of the foreign proteins 15. You have constructed an insulin-GST fusion protein and expressed it in E. coli. You want to separate the recombinant...
A Which of the following statements about Electromobility Shift Assays (EMSA) is correct? 1 EMSA gels...
A Which of the following statements about Electromobility Shift Assays (EMSA) is correct? 1 EMSA gels contain SDS detergent to maintain the shape of the of protein. 2 Large DNA molecules flow faster down the gel towards the positive pole in EMSA. 3 EMSA gels cannot be used to determine whether a particular protein has bound to a specific DNA sequence. 4 Smaller DNA molecules flow faster down the gel towards the positive pole in EMSA. B Which of the...
Sodium dodecylsulfate (SDS) plays an important role in SDS PAGE. Select each correct description of what...
Sodium dodecylsulfate (SDS) plays an important role in SDS PAGE. Select each correct description of what SDS does in denatured electrophoresis. Choose one or more: A. Because SDS is a detergent, it supports the native state by interacting with the nonpolar portions of a protein, stabilizing the three-dimensional structure of a protein. B. SDS is an amphipathic compound that binds to the hydrophobic portion of the protein, coating the mixture and giving the protein an overall negative charge proportional to...
1. Figure I shows an SDS-PAGE gel. A) Rank the 3 proteins by size, from largest...
1. Figure I shows an SDS-PAGE gel. A) Rank the 3 proteins by size, from largest to smallest. Explain why this trend is observed in SDS-PAGE gels. B) What is the purpose of SDS in SDS-PAGE? C) Sample L is the ladder. What is its purpose? D) Typically, PA (polyacrylamide) is used as the gel for protein electrophoresis, whereas agarose is used for DNA electrophoresis. Explain why a different gel material is used, Specifically referring to the pore size of...
32. Which of the following would make a protein of a large size move faster through...
32. Which of the following would make a protein of a large size move faster through an SDS gel electrophoresis separation? a. add more protein to your sample b. add more buffer c. remove some buffer d. decrease the acrylamide concentration of the gel e. increase the acrylamide concentration of the gel 33. Which of the following statements are accurate? i. SDS binds to proteins, introducing a negative charge which is proportional to the length of the protein primary structure....
Can someone help me answers these? These questions can have one answer, more than one answer,...
Can someone help me answers these? These questions can have one answer, more than one answer, or none. Which of the following factors directly affects the distance and speed of a migration of a protein during electrophoresis? - affinity of protein to agarose/polysaccharides - solubility of protein - shape of protein - function of a protein - size of protein (I chose the size of protein, and I got partial wrong 2/4) What is the function of sodium dodecyl sulfate...
Based on the migration of proteins A, B, and C in these gels, which of the following statements is correct? Cathode (-) Anode (+) Native SDS-PAGE Select one a. Protein B is larger and more positively charged than Protein A b. Protein C is smaller and more positively charged than protein B c. Protein A is a small protein with a high positive charge d. Protein A is a large protein with a low positive charge Your answer is incorrect.
Based on the migration of 3 DNA fragments {A, B, & C) of the indicated sizes (where kb = kilobases, ie thousand base pairs) in these gels, which of the following statements is correct? А В С А В С kb 0.5 Gel #1 Gel #2 Select one: a. Gell #1 has a higher % agarose than gel #2 b. An 8% acrylamide gel would give greater resolution of fragments larger than 500 bp than either of these gels. c....
I am confused on this question, the correct answer is A and I
chose B. I thought the cathode was positively charged, and the
anode was negateively charged; and a high PI would incicate a more
positive charge, and a low PI would incidate a more negative chare.
Are these correct or am I backwards in some these? Also, are any of
these different for a galvanic or electrolytic cell?
Please explain how you would answer this question, thank
you!...
Sodium dodecylsulfate (SDS) plays an important role in SDS PAGE. Select each correct description of what SDS does in denatured electrophoresis. Choose one or more: A. Because SDS is a detergent, it supports the native state by interacting with the nonpolar portions of a protein, stabilizing the three-dimensional structure of a protein. B. SDS is an amphipathic compound that binds to the hydrophobic portion of the protein, coating the mixture and giving the protein an overall negative charge proportional to...
1. Figure I shows an SDS-PAGE gel. A) Rank the 3 proteins by size, from largest to smallest. Explain why this trend is observed in SDS-PAGE gels. B) What is the purpose of SDS in SDS-PAGE? C) Sample L is the ladder. What is its purpose? D) Typically, PA (polyacrylamide) is used as the gel for protein electrophoresis, whereas agarose is used for DNA electrophoresis. Explain why a different gel material is used, Specifically referring to the pore size of...
32. Which of the following would make a protein of a large size move faster through an SDS gel electrophoresis separation? a. add more protein to your sample b. add more buffer c. remove some buffer d. decrease the acrylamide concentration of the gel e. increase the acrylamide concentration of the gel 33. Which of the following statements are accurate? i. SDS binds to proteins, introducing a negative charge which is proportional to the length of the protein primary structure....
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