Homework Answers
Gel filtration tells us about the total weight of the protein. It is 200 kD.
SDS PAGE denatures protein and gives band on the gel. We are getting one band of 100 kD. It means the protein has 2 subunits, 100 kD each.
After beta marcaptoethanol treatment, which is a reducing agent and breaks covalent (disulphide) bonds between peptide chain, we are getting 2 bands, 60 and 40 kD. It means one subunit of 100 kD contains two peptide chains, 60 and 40 kD both of which are joined by covalent protein.
Given protein = 2 subunits = (60 + 40) + (60 + 40)
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Sample problem: Protein structure Determine the subunit composition of a protein from the following information: •...
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.
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...
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 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)
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...
How can I do this problem step by step? How did they get the following answers?
How can I do this problem step by step? How did they get the
following answers?
SDS-PAGE Gel filtration in buffer Question 3 (9 pts) Referring to the data at the right, deduce the schematic structure of proteins A-C. At the right is the behavior of the8003 proteins on size exclusion chromatography Use the sample answer for the amount of detail 3a- required, show the quaternary structural arrangement including disulfide linkages (if appropriate) 230 <Da 60 kD 10 D Protein...
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...
A purified protein has a molecular mass of 360 kDa when measured by size exclusion chromatography....
A purified protein has a molecular mass of 360 kDa when measured by size exclusion chromatography. When analyzed by gel electrophoresis in the presence of SDS, three bands are observed, with molecular masses of 160, 140, and 60 kDa. When gel electrophoresis is carried out in the presence of SDS and dithiothreitol three bands are once again observed, with molecular masses of 140, 80, and 60 kDa. What is the subunit composition of the protein?
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.
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.
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 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)
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...
How can I do this problem step by step? How did they get the
following answers?
SDS-PAGE Gel filtration in buffer Question 3 (9 pts) Referring to the data at the right, deduce the schematic structure of proteins A-C. At the right is the behavior of the8003 proteins on size exclusion chromatography Use the sample answer for the amount of detail 3a- required, show the quaternary structural arrangement including disulfide linkages (if appropriate) 230 <Da 60 kD 10 D Protein...
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...
A purified protein has a molecular mass of 360 kDa when measured by size exclusion chromatography. When analyzed by gel electrophoresis in the presence of SDS, three bands are observed, with molecular masses of 160, 140, and 60 kDa. When gel electrophoresis is carried out in the presence of SDS and dithiothreitol three bands are once again observed, with molecular masses of 140, 80, and 60 kDa. What is the subunit composition of the protein?
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