Homework Answers
Urea disrupts the non covalent bonds between different polypeptide chains and mercaptowthanol reduces disulfide linkages. So the above mentioned data reveals that the protein consists of four polypeptide chains two each of 50 KD and other two of 40 and 60 KD.
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5. A protein has a molecular weight of 200 kD. On treatment with urea, two bands...
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.
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 is purified from a bacterium using Size Exclusion Chromatography (SEC), with a molecular weight...
A protein is purified from a bacterium using Size Exclusion Chromatography (SEC), with a molecular weight of 200kD. When this protein is run on SDS-PAGE , a sing band is observed at 100kD. Based on these observations, what can be concluded about the structure of the protein? The protein consist of two 200kD subiunits The protein has a quaternary structure The protein is madeup of two 100 kD subunits Proteins is a tetramer consisting of 200 kD domains. The protein...
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...
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.
4. The molecular weight of an Dalton, as determined by sedimentation equilibrium measurements and by gel...
4. The molecular weight of an Dalton, as determined by sedimentation equilibrium measurements and by gel filtration chromatography. The SDS-polyacrylamide gel electrophoresis (SDS PAGE) of the protein yields a single band corresponding to molecular weight of 70,000 Dalton. However, in the presence of the reducing agent, B-mercaptoethanol, the SDS PAGE shows two bands, corresponding to molecular weights of 30,000 and 20,000 Dalton. unspecified protein, at physiological conditions, is 70,000 ure a. From these data, describe the native protein in terms...
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...
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?
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 • 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 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.
4. The molecular weight of an Dalton, as determined by sedimentation equilibrium measurements and by gel filtration chromatography. The SDS-polyacrylamide gel electrophoresis (SDS PAGE) of the protein yields a single band corresponding to molecular weight of 70,000 Dalton. However, in the presence of the reducing agent, B-mercaptoethanol, the SDS PAGE shows two bands, corresponding to molecular weights of 30,000 and 20,000 Dalton. unspecified protein, at physiological conditions, is 70,000 ure a. From these data, describe the native protein in terms...
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...
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?
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....
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