Homework Answers
3a) a monomeric protein with a molecular weight of 35,000 Da.
Answer: Number of band = 1 and molecular weight of the band on SDS gel is 35 kilo dalton (KDa)
3b) a trimeric protein containing three chains, each with a molecular weight of 60,000 Da
Answer: Number of band = 1 and molecular weight of the band on SDS gel is 60 kilo dalton (KDa)
The three chains in the trimeric protein are joined by disulphide bonds which are broken in SDS PAGE to form three monomeric chain each of 60 KDa.
3c) Answer:
An immunoglobulin G has two light chain and two heavy chain ; both are linked by disulfide bonds. The IgG complex has molecular weight of 150 KDa. (25 KDa+25 KDa+50 KDa+50 KDa). As there is no reducing chemical in the gel,
Number of band = 1 and molecular weight of the band on SDS gel is 150 kilo dalton (KDa)
3d) IgG in a reducing gel
As Beta-Mercaptoethanol is added to the sample, it breaks all disulfide linkage present in the IgG. So all the light and heavy chains are separated and heavy chain also breaks into Fab and Fc region each having 25 KDa.
Number of band = 1 and molecular weight of the band on SDS gel is 25 kilo dalton (KDa)
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Predict the patterns (number of bands and apparent molecular weights) of the following proteins on SDS...
4. The molecular weight of an Dalton, as determined by sedimentation equilibrium measurements and by gel...
4. The molecular weight of an Dalton, as determined by sedimentation equilibrium measurements and by gel filtration chromatography. The SDS-polyacrylamide gel electrophoresis (SDS PAGE) of the protein yields a single band corresponding to molecular weight of 70,000 Dalton. However, in the presence of the reducing agent, B-mercaptoethanol, the SDS PAGE shows two bands, corresponding to molecular weights of 30,000 and 20,000 Dalton. unspecified protein, at physiological conditions, is 70,000 ure a. From these data, describe the native protein in terms...
SDS Page Gel: The provided standard protein sample for electrophoresis consists of 9 polypeptides with molecular...
SDS Page Gel:
The provided standard protein sample for electrophoresis
consists of 9 polypeptides with molecular weights ranging from 250
to 15 KDa.
Sample 1: Protein A in a sample buffer with
B-Mercaptoethanol
Sample 2: Protein A in a sample buffer without
B-Mercaptoethanol
Sample 3: Protein B in a sample buffer with
B-Mercaptoethanol
Sample 4: Protein C in a sample buffer without
B-Mercaptoethanol
Use the picture below & the information about the proteins
above to answer the following questions.
1a....
5. A native protein has a molecular weight of 150,000 Da. Denaturing SDS electrophoresis results in...
5. A native protein has a molecular weight of 150,000 Da. Denaturing SDS electrophoresis results in two bands with molecular weights of approximately 53,000 and 23,000 Da. What arrangement of polypeptide chains in the native protein would best explain these results? 2. If two proteins have the same molecular weight, are they necessarily the same protein? Can you definitely assign the identity of a protein based on its molecular weight? Why or why not?
A protein sample complex consists of two proteins, a smaller protein, X, and a larger protein,...
A protein sample complex consists of two proteins, a smaller protein, X, and a larger protein, Y. Protein X is composed of two polypeptide chains linked by disulfide bonds. Protein Y is composed of three polypeptide chains linked by disulfide bonds. The complex is analyzed by native PAGE, reducing SDS-PAGE and non-reducing SDS-PAGE. Native PAGE does not include sodium dodecyl sulfate, or SDS. Reducing SDS-PAGE uses both SDS and a reducing agent in the buffer. Non-reducing SDS-PAGE uses SDS, but...
Chapter 3 Home Active and Due Dates Chapter Homework Resouros Ghve Up! Feedback PAGE A protein...
Chapter 3 Home Active and Due Dates Chapter Homework Resouros Ghve Up! Feedback PAGE A protein sample complex consists of two proteins, a smaller protein, X, and a larger protein, Y. Protein X is composed two polypeptide chains linked by disulfide bonds. Protein Y is composed of three polypeptide chain linked by disulfide bonds The complex is analyzed by native PAGE, reducing SDS-PAGE and non-reducing SDS-PAGE Native PAGE does not include sodium dodecyl sulfate, or SDS. Reducing SDS-PAGE uses both...
Why are proteins heat denatured prior to analysis in SDS-PAGE? Select all answers that apply. Denaturation...
Why are proteins heat denatured prior to analysis in SDS-PAGE? Select all answers that apply. Denaturation of the protein is necessary so that proteins run proportionally to their size, based on the interaction of SDS with the unfolded protein. Heat is used to hydrolyze the peptide bonds of the protein. The heat step allows the proteins to unfold, enabling the protein chain to be coated with SDS molecules. Heat is used to hydrolyze disulfide bonds. QUESTION 2 1.5 points Saved...
a-d plz 7. Protein purification. As a graduate student, the first protein I purified was RNA...
a-d plz
7. Protein purification. As a graduate student, the first protein I purified was RNA polymerase (RNAP) from E. coli- Some physical and chemical properties of Ecoli RNAP Molecular max470,000 g/mol polynentide compasitian (subunits): (50 kDa), k andok a pl = 5.34 substrates: NTPs cofactor: Mg? Purification protocol. E coli cells were broken usine Isozyme, yielding a cellualar extract containing a protcome solution 4M (NHOSO, was added to the cellular extract. A white protein precipitate was formed incuding RNAM...
7. Protein purification. As a graduate student, the first protein I purified was RNA polymerase (RNAP)...
7. Protein purification. As a graduate student, the first protein I purified was RNA polymerase (RNAP) from E. coli. Some physical and chemical properties of E. coli RNAP Molecular mass = 470,000 g/mol polypeptide composition (subunits): a (50 kDa), B (150 kDa) and 6 (70 kDa) pl = 5.34 substrates: NTPS cofactor: Mg Purification protocol. E. coli cells were broken using lysozyme, yielding a cellualar extract containing a proteome solution. 4M (NH4)2SO4 was added to the cellular extract. A white...
1. A novel protein is described that functions best at pH 11.5 (!), and contains a...
1. A novel protein is described that functions best at pH 11.5 (!), and contains a loop between helix 2 and helix 5 of the protein. The authors report that at pH 11.5 this loop is stabilized by formation of a salt bridge between two amino acid side chains. a. Which of the following amino acid pairs would be the best candidates for this interaction and why: GlnCys, Tyr-Arg, or His-Asp. b. Show the full amino acid structures and interactions...
i need help with the whole page! 8. You try to ligate a cDNA fragment with...
i
need help with the whole page!
8. You try to ligate a cDNA fragment with Bgl Il and Xho I sticky ends into the Bgl Il and Xho I sites in the multi- cloning site of a vector (vector plus insert: 7 kbp). The plasmid vector has an ampicillin resistance gene. What do you see on the plate next day if you spread the transformed bacteria on an LB agar plate with ampicillin- (1) bacteria with no vector, (2)...
4. The molecular weight of an Dalton, as determined by sedimentation equilibrium measurements and by gel filtration chromatography. The SDS-polyacrylamide gel electrophoresis (SDS PAGE) of the protein yields a single band corresponding to molecular weight of 70,000 Dalton. However, in the presence of the reducing agent, B-mercaptoethanol, the SDS PAGE shows two bands, corresponding to molecular weights of 30,000 and 20,000 Dalton. unspecified protein, at physiological conditions, is 70,000 ure a. From these data, describe the native protein in terms...
SDS Page Gel:
The provided standard protein sample for electrophoresis
consists of 9 polypeptides with molecular weights ranging from 250
to 15 KDa.
Sample 1: Protein A in a sample buffer with
B-Mercaptoethanol
Sample 2: Protein A in a sample buffer without
B-Mercaptoethanol
Sample 3: Protein B in a sample buffer with
B-Mercaptoethanol
Sample 4: Protein C in a sample buffer without
B-Mercaptoethanol
Use the picture below & the information about the proteins
above to answer the following questions.
1a....
5. A native protein has a molecular weight of 150,000 Da. Denaturing SDS electrophoresis results in two bands with molecular weights of approximately 53,000 and 23,000 Da. What arrangement of polypeptide chains in the native protein would best explain these results? 2. If two proteins have the same molecular weight, are they necessarily the same protein? Can you definitely assign the identity of a protein based on its molecular weight? Why or why not?
A protein sample complex consists of two proteins, a smaller protein, X, and a larger protein, Y. Protein X is composed of two polypeptide chains linked by disulfide bonds. Protein Y is composed of three polypeptide chains linked by disulfide bonds. The complex is analyzed by native PAGE, reducing SDS-PAGE and non-reducing SDS-PAGE. Native PAGE does not include sodium dodecyl sulfate, or SDS. Reducing SDS-PAGE uses both SDS and a reducing agent in the buffer. Non-reducing SDS-PAGE uses SDS, but...
Chapter 3 Home Active and Due Dates Chapter Homework Resouros Ghve Up! Feedback PAGE A protein sample complex consists of two proteins, a smaller protein, X, and a larger protein, Y. Protein X is composed two polypeptide chains linked by disulfide bonds. Protein Y is composed of three polypeptide chain linked by disulfide bonds The complex is analyzed by native PAGE, reducing SDS-PAGE and non-reducing SDS-PAGE Native PAGE does not include sodium dodecyl sulfate, or SDS. Reducing SDS-PAGE uses both...
Why are proteins heat denatured prior to analysis in SDS-PAGE? Select all answers that apply. Denaturation of the protein is necessary so that proteins run proportionally to their size, based on the interaction of SDS with the unfolded protein. Heat is used to hydrolyze the peptide bonds of the protein. The heat step allows the proteins to unfold, enabling the protein chain to be coated with SDS molecules. Heat is used to hydrolyze disulfide bonds. QUESTION 2 1.5 points Saved...
a-d plz
7. Protein purification. As a graduate student, the first protein I purified was RNA polymerase (RNAP) from E. coli- Some physical and chemical properties of Ecoli RNAP Molecular max470,000 g/mol polynentide compasitian (subunits): (50 kDa), k andok a pl = 5.34 substrates: NTPs cofactor: Mg? Purification protocol. E coli cells were broken usine Isozyme, yielding a cellualar extract containing a protcome solution 4M (NHOSO, was added to the cellular extract. A white protein precipitate was formed incuding RNAM...
7. Protein purification. As a graduate student, the first protein I purified was RNA polymerase (RNAP) from E. coli. Some physical and chemical properties of E. coli RNAP Molecular mass = 470,000 g/mol polypeptide composition (subunits): a (50 kDa), B (150 kDa) and 6 (70 kDa) pl = 5.34 substrates: NTPS cofactor: Mg Purification protocol. E. coli cells were broken using lysozyme, yielding a cellualar extract containing a proteome solution. 4M (NH4)2SO4 was added to the cellular extract. A white...
i
need help with the whole page!
8. You try to ligate a cDNA fragment with Bgl Il and Xho I sticky ends into the Bgl Il and Xho I sites in the multi- cloning site of a vector (vector plus insert: 7 kbp). The plasmid vector has an ampicillin resistance gene. What do you see on the plate next day if you spread the transformed bacteria on an LB agar plate with ampicillin- (1) bacteria with no vector, (2)...
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