Proteins: BSA, yeast ADH, ovalbumin, lysozyme
. Discuss how you were able to determine which
protein was in which lane. You will have to do some
online research to find the molecular weight of each protein,
whether it is a dimer, etc. For at least one of the proteins, there
is some variability regarding the molecular weight, but the range
should still allow you to determine which lane each of the proteins
is in. For each lane, pay attention to the most prominent
band(s).
PLEASE EXPLAIN WHAT EXTRA INFO IS NEEDED...
the proteins (BSA, yeast ADH, ovalbumin, lysozyme) need to be
identified, through the blue picture of the lanes, and explained
how they were determined.
Homework Answers
Answer- to determine that which protein was present in which lane the standard protein ladder should be used for the comparison. The bands corresponding to the distance travelled by the standard samples will be used to compare. The bands will be differentiated upon the basis of the distance travelled and the location they share with the standard protein ladder.
Add Answer to:
Proteins: BSA, yeast ADH, ovalbumin, lysozyme
. Discuss how you were able to determine which
protein...
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...
6. A series of proteins of known mass were running over a Sephacryl S300 column. A....
6. A series of proteins of known mass were running over a Sephacryl S300 column. A. Determine the molecular mass of the unknown protein. B. Give a plausible explanation for the strange behavior of ferritin’s elution from the column. How would you test your idea? Protein Mr (kDa) Ve (mL) Blue dextran 1000 85 Lysozyme 14 200 Chymotrypsinogin 25 190 Ovalbumin 45 170 BSA 65 150 Aldolase 150 125 Urease 500 90 Ferritin 700 92 Ovomucoid 28 160 unknown ??...
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...
Betergents h. What chemical would you add to refold this protein? 16. You wish to purify...
Betergents h. What chemical would you add to refold this protein? 16. You wish to purify a novel protein from mammalian cells. You do not know this protein's size or charge, and are thus unsure of which steps to take. Fortunately, an antibody for this protein is available. You have two cell lines: one that expresses the protein, and one • that does not. . ) 4 5 III111 You run both cell lines on an SDS-PAGE (A) followed by...
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....
Sample 1: Protein A in a sample buffer with B-Mercaptoethanol. Sample 2 Protein A in a...
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. A. Fill the table below, based on the characteristics of the proteins and the components of the sample buffer. (12 points) Sample 1 Sample 2 Sample 3 Sample 4 Molecular weight 55 kn | 55k Da 52 +57 KDA 5257...
Confused on how to answer questions E, F, and G. The answer for E is Cysteine,...
Confused on how to answer
questions E, F, and G.
The answer for E is Cysteine,
F (i) is 2
F (ii) is 2
F (iii) is 180
Question 5. Protein X, a protein that binds tyrosine tightly, can be purified in three chromatography steps: 1) affinity chromatography using a tyrosine resin, 2) gel filtration chromatography using a resin with a separation range of 30-200 kDa, and 3) anion exchange chromatography run at pH 7.6. The elution profiles for Steps...
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,...
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...
2) A blotting method known as Western blotting can be used to detect proteins that are...
2) A blotting method known as Western blotting can be used to detect proteins that are translated from a particular mRNA This techniques first separates proteins by size using electrophoresis then detects specific proteins through staining (antibody directed). Key is that you can visualize only the protein of interest on the gel. Suppose a researcher was interested in the effects of mutations on the expression of a gene that encodes protein X This protein is expressed in the skin and...
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...
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...
Betergents h. What chemical would you add to refold this protein? 16. You wish to purify a novel protein from mammalian cells. You do not know this protein's size or charge, and are thus unsure of which steps to take. Fortunately, an antibody for this protein is available. You have two cell lines: one that expresses the protein, and one • that does not. . ) 4 5 III111 You run both cell lines on an SDS-PAGE (A) followed by...
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....
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. A. Fill the table below, based on the characteristics of the proteins and the components of the sample buffer. (12 points) Sample 1 Sample 2 Sample 3 Sample 4 Molecular weight 55 kn | 55k Da 52 +57 KDA 5257...
Confused on how to answer
questions E, F, and G.
The answer for E is Cysteine,
F (i) is 2
F (ii) is 2
F (iii) is 180
Question 5. Protein X, a protein that binds tyrosine tightly, can be purified in three chromatography steps: 1) affinity chromatography using a tyrosine resin, 2) gel filtration chromatography using a resin with a separation range of 30-200 kDa, and 3) anion exchange chromatography run at pH 7.6. The elution profiles for Steps...
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...
2) A blotting method known as Western blotting can be used to detect proteins that are translated from a particular mRNA This techniques first separates proteins by size using electrophoresis then detects specific proteins through staining (antibody directed). Key is that you can visualize only the protein of interest on the gel. Suppose a researcher was interested in the effects of mutations on the expression of a gene that encodes protein X This protein is expressed in the skin and...
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