A protein gives two bands of 50 and 80 kD on SDS PAGE. Treatment with 2-mercaptoethanol...
A protein gives two bands of 50 and 80 kD on SDS PAGE. Treatment with 2-mercaptoethanol gives two bands of 50kD and 40kD. Give detailed information about this protein including its molecular weight.
Homework Answers
SDS PAGE denatures proteins and tells us about the number of subunits present in it. So, in the given protein, there are two subunits, each of 50 kD and 80 kD.
Beta mercaptoethanol breaks disulfide (covalent) bond present between peptide chains. We can see that 50 kD fragement which was obtained after denaturation is also present here. So, it has remain unchanged. But instead of 80 kD, we have 40 kD band now. It means disulfide bonds are present between the two peptide chains, each of 40 kD.
Final protein = 2 subunits
1st subunit = 50 kD
2nd subunit = 2 peptide chains of 40 kD each, joined by disulfide bonds
Final protein weight = 50 + 40 + 40 = 130 kD
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A protein gives two bands of 50 and 80 kD on SDS PAGE. Treatment
with 2-mercaptoethanol...
Sample problem: Protein structure • A protein gives two bands of 50 and 80 kD on...
Sample problem: Protein structure • A protein gives two bands of 50 and 80 kD on SDS PAGE. Treatment with 2-mercaptoethanol gives two bands of 50kD and 40kD. Give detailed information about this protein including its molecular weight.
Sample problem: Protein structure • A protein gives two bands of 50 and 80 kD on...
Sample problem: Protein structure • A protein gives two bands of 50 and 80 kD on SDS PAGE. Treatment with 2-mercaptoethanol gives two bands of 50kD and 40kD. Give detailed information about this protein including its molecular weight.
5. A protein has a molecular weight of 200 kD. On treatment with urea, two bands...
5. A protein has a molecular weight of 200 kD. On treatment with urea, two bands of 100kD and 50kD are obtained in SDS PAGE. After treatment with 2-mercaptoethanol, three bands of 40, 60 kD and 50KD are obtained. What information about the quaternary structure of the protein can be obtained? (5 marks)
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....
Carl has just finished purifying a protein and analysis by gel filtration indicated that the molecular...
Carl has just finished purifying a protein and analysis by gel filtration indicated that the molecular weight of the native (undenatured) protein was 130,000 dalton. His advisor wanted him to determine whether this protein had quaternary structure using gel electrophoresis. He wants to be able to describe the molecular weight of each of the subunits and the forces involved in linking these subunits together (disulfide linkages and/or electrostatic, hydrogen bonding and hydrophobic interactions). Carl first analyzed his pure protein sample...
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?
1. When using SDS-PAGE, proteins will be separated on the basis of what physical property? 2. ...
1. When using SDS-PAGE, proteins will be separated on the basis of what physical property? 2. You are given two proteins, one with a molecular weight of 67,435 Daltons and other with a molecular weight of 21,345 Daltons. Which protein will move further in the SDS-PAGE?
Please address both of the underlined points in your answer. 09 (0) (10 points) A protein...
Please address both of the underlined points in your
answer.
09 (0) (10 points) A protein was purified and then analyzed on a size exclusion column. Its MW was determined to be 110.000 Dalton. The SDS-PAGE gel shows two bands, corresponding to molecular weights of 35,000 and 20,000 Dalton. Describe the native conformation of this protein in terms of the number of subunits present and their molecular weight. (2)
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...
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...
Sample problem: Protein structure • A protein gives two bands of 50 and 80 kD on SDS PAGE. Treatment with 2-mercaptoethanol gives two bands of 50kD and 40kD. Give detailed information about this protein including its molecular weight.
Sample problem: Protein structure • A protein gives two bands of 50 and 80 kD on SDS PAGE. Treatment with 2-mercaptoethanol gives two bands of 50kD and 40kD. Give detailed information about this protein including its molecular weight.
5. A protein has a molecular weight of 200 kD. On treatment with urea, two bands of 100kD and 50kD are obtained in SDS PAGE. After treatment with 2-mercaptoethanol, three bands of 40, 60 kD and 50KD are obtained. What information about the quaternary structure of the protein can be obtained? (5 marks)
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?
Please address both of the underlined points in your
answer.
09 (0) (10 points) A protein was purified and then analyzed on a size exclusion column. Its MW was determined to be 110.000 Dalton. The SDS-PAGE gel shows two bands, corresponding to molecular weights of 35,000 and 20,000 Dalton. Describe the native conformation of this protein in terms of the number of subunits present and their molecular weight. (2)
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...
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...
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