Homework Answers
Answer has been attached below . Answer is based on results provided by you in table. Hope this will help.
P
c) SDS page is done to detect
presence of subunit or state of oligomerization of protein. SDS
page , contains beta mercaptoethanol which reduces disulphide bonds
present in protein.
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Sample 1: Protein A in a sample buffer with B-Mercaptoethanol. Sample 2 Protein A in a...
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 problem: Protein structure Determine the subunit composition of a protein from the following information: •...
Sample problem: Protein structure Determine the subunit composition of a protein from the following information: • Molecular mass by Gel filtration: 200kD • Molecular mass by SDS PAGE: 100kD • Molecular mass by SDS PAGE with 2- mercaptoethanol: 40 kD and 60 kD.
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...
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...
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.
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...
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.
(3) The 2x sample buffer contains SDS and B-mercaptoethanol. What are their functions? (1 pt) (4)...
(3) The 2x sample buffer contains SDS and B-mercaptoethanol. What are their functions? (1 pt) (4) What samples would you load on the gel besides the purified plant protein? Explain your reasons for loading those samples. (2 pts) (Hint: In this lab you loaded Ladder, BEW, pool A, and pool B. Only pool B contains the purified protein, but why do we need to load all the other samples? Same principles should apply to this question for the plant protein.)...
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...
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 problem: Protein structure Determine the subunit composition of a protein from the following information: • Molecular mass by Gel filtration: 200kD • Molecular mass by SDS PAGE: 100kD • Molecular mass by SDS PAGE with 2- mercaptoethanol: 40 kD and 60 kD.
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...
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...
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.
(3) The 2x sample buffer contains SDS and B-mercaptoethanol. What are their functions? (1 pt) (4) What samples would you load on the gel besides the purified plant protein? Explain your reasons for loading those samples. (2 pts) (Hint: In this lab you loaded Ladder, BEW, pool A, and pool B. Only pool B contains the purified protein, but why do we need to load all the other samples? Same principles should apply to this question for the plant protein.)...
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...
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