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A protein sample complex consists of two proteins, a smaller protein, X, and a larger protein,...
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...
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....
Predict the patterns (number of bands and apparent molecular weights) of the following proteins on SDS...
Predict the patterns (number of bands and apparent molecular weights) of the following proteins on SDS gels: a. A monomeric protein with a molecular weight of 35,000 Da b. A trimetric protein containing three chains, each with a molecular weight of 60,000 Da c. Immunoglobulin G (Nelson and Cox, page 178) in a non-reducing gel (no beta -mercaptoethanol added in the sample solution) - the light chains have a molecular weight of 25,000 Da and the heavy chains 50,000 Da...
Two different experiments were performed to determine the quaternary structure of HCV reverse transcriptase as well...
Two different experiments were performed to determine
the quaternary structure of HCV reverse transcriptase as well as
the molecular size of each subunit. In these experiments, HCV
reverse transcriptase was mixed with equal masses of two proteins
with known molecular weights of 10 KDa and 80 KDa. Both of these
proteins consisted of a
single polypeptide chain. This mixture was then separated by gel
filtration (below) or by SDS-PAGE (below).
Gel Filtration Column: The absorption as a function of the...
You have a mixture of three proteins, Huskerase (pI=6.5), Gopherase (pI=8.6), and Badgerase (pI= 4.6), which...
You have a mixture of three proteins, Huskerase (pI=6.5), Gopherase (pI=8.6), and Badgerase (pI= 4.6), which you would like to separate by chromatographic technique(s). A native gel indicates that the three proteins have approximate molecular weights of 240 kDa, 215 kDa, and 79 kDa respectively. a) Based on this information, describe an appropriate separation strategy using chromatography. Be sure to indicate relevant conditions (pH, resin(s), etc). b) Given that Huskerase is a homotrimer, Gopherase a heterotetramer, and Badgerase a homodimer,...
You develop a scheme to purify the protein RANIN, and use your "sequencing toolbox" to identify...
You develop a scheme to purify the protein RANIN, and use your "sequencing toolbox" to identify it. You suspect RANIN has quaternary structure, but the polypeptides are not separated by extreme pH. Suggest another method SDS-PAGE samples run with and without reducing agent tefis you RANIN does not have intermolecular disulfide bonds, but it is made up of two distinct polypeptide chains. Draw the SDS-PAGE results and explain how you know. RANIN chain A has a pi of approximately 9,...
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...
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-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...
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...
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...
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....
Predict the patterns (number of bands and apparent molecular weights) of the following proteins on SDS gels: a. A monomeric protein with a molecular weight of 35,000 Da b. A trimetric protein containing three chains, each with a molecular weight of 60,000 Da c. Immunoglobulin G (Nelson and Cox, page 178) in a non-reducing gel (no beta -mercaptoethanol added in the sample solution) - the light chains have a molecular weight of 25,000 Da and the heavy chains 50,000 Da...
Two different experiments were performed to determine
the quaternary structure of HCV reverse transcriptase as well as
the molecular size of each subunit. In these experiments, HCV
reverse transcriptase was mixed with equal masses of two proteins
with known molecular weights of 10 KDa and 80 KDa. Both of these
proteins consisted of a
single polypeptide chain. This mixture was then separated by gel
filtration (below) or by SDS-PAGE (below).
Gel Filtration Column: The absorption as a function of the...
You develop a scheme to purify the protein RANIN, and use your "sequencing toolbox" to identify it. You suspect RANIN has quaternary structure, but the polypeptides are not separated by extreme pH. Suggest another method SDS-PAGE samples run with and without reducing agent tefis you RANIN does not have intermolecular disulfide bonds, but it is made up of two distinct polypeptide chains. Draw the SDS-PAGE results and explain how you know. RANIN chain A has a pi of approximately 9,...
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...
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...
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