Homework Answers
Yes, the addition of beta mercaptoethanol to an SDS treated protein always results in a different protein band pattern than if the same protein was only with SDS.
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Does the addition of B-mercaptoethanol to an SDS treated protein always result in a different protein...
A scientist subjects the mixture to denaturing Electrophoresis (SDS-PAGE) but forgets to include -mercaptoethanol in the...
A scientist subjects the mixture to denaturing Electrophoresis (SDS-PAGE) but forgets to include -mercaptoethanol in the sample buffer. The Coomassie-stained gel has only three bands as seen at right. a) Identify each sample band by labeling with the appropriate letters b)Provide an explanation for i) The number of bands ii) The apparent molecular weight indicated by the band mobilities
(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.)...
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...
After performing SDS-PAGE of a protein extract, there will be a number of protein “bands” in...
After performing SDS-PAGE of a protein extract, there will be a number of protein “bands” in a lane of the gel. In a single “band” all proteins have the same A.native (i.e. original) charge B. function C. molecular mass
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...
Why are proteins heat denatured prior to analysis in SDS-PAGE? Select all answers that apply. Denaturation...
Why are proteins heat denatured prior to analysis in SDS-PAGE? Select all answers that apply. Denaturation of the protein is necessary so that proteins run proportionally to their size, based on the interaction of SDS with the unfolded protein. Heat is used to hydrolyze the peptide bonds of the protein. The heat step allows the proteins to unfold, enabling the protein chain to be coated with SDS molecules. Heat is used to hydrolyze disulfide bonds. QUESTION 2 1.5 points Saved...
What is the purpose of SDS? ***To Make the protein negative was not an option What...
What is the purpose of SDS? ***To Make the protein negative was not an option What will happen if you remove SDS from SDS PAGE? What are the products of light dependent and light independent reactions? Why does absorbance decrease when you add DCPIP to cholorplast and use light ? Where would you find LHCII ? Which of the following is true about abtibodies? None! What will happen if you put the gel against the positive pole and the membrane...
Part Il Short Amwer Oestions and Problem. There are total of sixty-four 64 10 How does...
Part Il Short Amwer Oestions and Problem. There are total of sixty-four 64 10 How does a protein's amino acid sequence infonce the tertiary structure 5 Points le prints in this section 11. A protein was purified to homogeneity. Determination of the mass by gel-filtration chromatography yields 30 d. Gel-fturation chromatography in the presence of 6 Murea yields a 117.d species and a 22-d species. The same protein was treated with mM B-mercaptoethanol and analyzed using SDS-PAGE. There were hands...
Please Help with simple explanation .. please answer at least the last 3 questions if can't...
Please Help with simple
explanation ..
please answer at least the last 3 questions if can't estimate ,,
please answer the first Q only
3654 Biochemistry Expt. 7 (cont.) Name with reducing agents A B A B (5pts) Protein A contains 2 polypeptide chains (1 of 70,000, 1 of 35,000) held together by disulfide bonds. Protein B contains 2 polypeptide chains (each -75,000) held together by hydrophobic interactions and electrostatic forces. On the SDS-PAGE gel to the right, sketch the...
A scientist subjects the mixture to denaturing Electrophoresis (SDS-PAGE) but forgets to include -mercaptoethanol in the sample buffer. The Coomassie-stained gel has only three bands as seen at right. a) Identify each sample band by labeling with the appropriate letters b)Provide an explanation for i) The number of bands ii) The apparent molecular weight indicated by the band mobilities
(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.)...
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...
Why are proteins heat denatured prior to analysis in SDS-PAGE? Select all answers that apply. Denaturation of the protein is necessary so that proteins run proportionally to their size, based on the interaction of SDS with the unfolded protein. Heat is used to hydrolyze the peptide bonds of the protein. The heat step allows the proteins to unfold, enabling the protein chain to be coated with SDS molecules. Heat is used to hydrolyze disulfide bonds. QUESTION 2 1.5 points Saved...
Part Il Short Amwer Oestions and Problem. There are total of sixty-four 64 10 How does a protein's amino acid sequence infonce the tertiary structure 5 Points le prints in this section 11. A protein was purified to homogeneity. Determination of the mass by gel-filtration chromatography yields 30 d. Gel-fturation chromatography in the presence of 6 Murea yields a 117.d species and a 22-d species. The same protein was treated with mM B-mercaptoethanol and analyzed using SDS-PAGE. There were hands...
Please Help with simple
explanation ..
please answer at least the last 3 questions if can't estimate ,,
please answer the first Q only
3654 Biochemistry Expt. 7 (cont.) Name with reducing agents A B A B (5pts) Protein A contains 2 polypeptide chains (1 of 70,000, 1 of 35,000) held together by disulfide bonds. Protein B contains 2 polypeptide chains (each -75,000) held together by hydrophobic interactions and electrostatic forces. On the SDS-PAGE gel to the right, sketch the...
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