Which technique could be used for molecular weight determinations in proteins under all circumstances? a.) gel...
Which technique could be used for molecular weight determinations in proteins under all circumstances?
a.) gel filtration b.) isoelectric focusing c.) carboxymethyl (CM) cellulose chromatography d.) a and e e.) SDS-PAGE
Homework Answers
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Which technique could be used for molecular weight
determinations in proteins under all circumstances?
a.) gel...
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...
1) Which technique separates molecules on the basis of molecular weight? * O Gel filtration O...
1) Which technique separates molecules on the basis of molecular weight? * O Gel filtration O Affinity chromatography O Cation exchange O Anion exchange 2) A molecule that contains a hydrophobic region as well as an adjacent hydrophilic region would be most accurately called* O Hygroscopic O Amphipathic O Polar O Non-polar
6. You are given a mixture of proteins that you analyze by standard 2-D electrophoresis, with...
6. You are given a mixture of proteins that you analyze by standard 2-D electrophoresis, with the following results for isoelectric points and apparent molecular weights: protein A (Mr 110,400; pl 4.60), protein B (Mr 10,100; pl 6.93), protein C (Mr 65,200; pI 7.84), and protein D (M 25,000; pI 8.15) a. After the 2-D separation, which protein will be in the upper left quadrant of the gel. given that e cathode-proximal end of the isoelectric focusing gel was on...
please help Tor F. A) High molecular weight proteins will migrate farther during gel electrophoresis (SDS-PAGE)....
please help
Tor F. A) High molecular weight proteins will migrate farther during gel electrophoresis (SDS-PAGE). d) B-sheet protein structures can be stabilized by hydrogen bonding between distant residues on the same polypeptide. e) B-sheets are a type of secondary structure and are found in every protein.
Exercise IV. Fill in the Blank 1. The method of Centrifugation, polyacrylamide gel electrophoresis, western blotting,...
Exercise IV. Fill in the Blank 1. The method of Centrifugation, polyacrylamide gel electrophoresis, western blotting, affinity purification) is the most widely used technique for determining the approximate molecular weight of a protein. 2. (Centrifugation, affinity chromatography, sonication, gel electrophoresis) is a method in which macromolecules are separated due to their size, charge, and other physical properties 3. SDS-PAGE is a form of electrophoresis in the presences of a/an (acidic solution, basic solution, anionic detergent, cationic detergent). 4. SDS not...
4. (Challenge) You are purifying a protein from the brain of patients with an unusual type of...
4. (Challenge) You are purifying a protein from the brain of patients with an unusual type of dementia triggered by a coronavirus and you hypothesize that this protein may be a signature molecule of this type of dementia. To pursue this hypothesis, you collect brain tissue from patients post mortem, do differential centrifugation, density gradient centrifugation, CM (carboxymethyl cellulose) ion exchange chromatography and gel filtration. You then assess the purity of your protein using both native and SDS gel electrophoresis. The...
__________ In a mixture of 4 proteins listed below, which one should elute the last in...
__________ In a mixture of 4 proteins listed below, which one should elute the last in size-exclusion chromatography: (A) Cytochrome, Mw - 13,000: (B) RNA polymerase, MW - 450,000 (C) 1gG Antibody, MW - 145,000: (D) Serum Albumin, MW - 68, 500 ______ Which of the following inhibition can be overcome by increasing the substrate concentration: (A) Feedback (product) inhibition (B) uncompetitive inhibition (C) Competitive inhibition (D) Noncompetitive inhibition __________ Which of the following separation techniques of proteins is based...
what is the principle of gel filtration chromatography? 19 E 3 2 1 AaBbceDdEe ABCDdee AaBbCcDc...
what is the principle of gel filtration chromatography?
19 E 3 2 1 AaBbceDdEe ABCDdee AaBbCcDc AaBbCcDdE No Spacing Heading 1 Heading 2 7. A. What is the principle of Gel filtration chromatography? (1 point) B. In gel filtration chromatography, what is the stationary phase and the mobile phase (that we used in our lab experiment)? (1 point) C. In what order would the proteins elute from a size exclusion column (limit 50- 40,000) (1 point) Protein Molecular weight KDa...
32. Which of the following would make a protein of a large size move faster through...
32. Which of the following would make a protein of a large size move faster through an SDS gel electrophoresis separation? a. add more protein to your sample b. add more buffer c. remove some buffer d. decrease the acrylamide concentration of the gel e. increase the acrylamide concentration of the gel 33. Which of the following statements are accurate? i. SDS binds to proteins, introducing a negative charge which is proportional to the length of the protein primary structure....
17) Consider the following experimental methods that are commonly used in biochemistry: A) dynamic light scattering....
17) Consider the following experimental methods that are commonly used in biochemistry: A) dynamic light scattering. B) polycrylamide gel electrophoresis (PAGE) with SDS present. C) polycrylamide gel electrophoresis (PAGE) without SDS present. D) surface plasmon resonance (SPR) E) differential scanning fluorimetry (DSF) F) analytical ultracentrifugation (equilibrium type) G) gel filtration chromatography (a) Which three of the methods are best for providing an estimate of the molecular weight of a protein in solution, in its native (non-denatured) form? (3 pts) Write...
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...
1) Which technique separates molecules on the basis of molecular weight? * O Gel filtration O Affinity chromatography O Cation exchange O Anion exchange 2) A molecule that contains a hydrophobic region as well as an adjacent hydrophilic region would be most accurately called* O Hygroscopic O Amphipathic O Polar O Non-polar
6. You are given a mixture of proteins that you analyze by standard 2-D electrophoresis, with the following results for isoelectric points and apparent molecular weights: protein A (Mr 110,400; pl 4.60), protein B (Mr 10,100; pl 6.93), protein C (Mr 65,200; pI 7.84), and protein D (M 25,000; pI 8.15) a. After the 2-D separation, which protein will be in the upper left quadrant of the gel. given that e cathode-proximal end of the isoelectric focusing gel was on...
please help
Tor F. A) High molecular weight proteins will migrate farther during gel electrophoresis (SDS-PAGE). d) B-sheet protein structures can be stabilized by hydrogen bonding between distant residues on the same polypeptide. e) B-sheets are a type of secondary structure and are found in every protein.
Exercise IV. Fill in the Blank 1. The method of Centrifugation, polyacrylamide gel electrophoresis, western blotting, affinity purification) is the most widely used technique for determining the approximate molecular weight of a protein. 2. (Centrifugation, affinity chromatography, sonication, gel electrophoresis) is a method in which macromolecules are separated due to their size, charge, and other physical properties 3. SDS-PAGE is a form of electrophoresis in the presences of a/an (acidic solution, basic solution, anionic detergent, cationic detergent). 4. SDS not...
__________ In a mixture of 4 proteins listed below, which one should elute the last in size-exclusion chromatography: (A) Cytochrome, Mw - 13,000: (B) RNA polymerase, MW - 450,000 (C) 1gG Antibody, MW - 145,000: (D) Serum Albumin, MW - 68, 500 ______ Which of the following inhibition can be overcome by increasing the substrate concentration: (A) Feedback (product) inhibition (B) uncompetitive inhibition (C) Competitive inhibition (D) Noncompetitive inhibition __________ Which of the following separation techniques of proteins is based...
what is the principle of gel filtration chromatography?
19 E 3 2 1 AaBbceDdEe ABCDdee AaBbCcDc AaBbCcDdE No Spacing Heading 1 Heading 2 7. A. What is the principle of Gel filtration chromatography? (1 point) B. In gel filtration chromatography, what is the stationary phase and the mobile phase (that we used in our lab experiment)? (1 point) C. In what order would the proteins elute from a size exclusion column (limit 50- 40,000) (1 point) Protein Molecular weight KDa...
32. Which of the following would make a protein of a large size move faster through an SDS gel electrophoresis separation? a. add more protein to your sample b. add more buffer c. remove some buffer d. decrease the acrylamide concentration of the gel e. increase the acrylamide concentration of the gel 33. Which of the following statements are accurate? i. SDS binds to proteins, introducing a negative charge which is proportional to the length of the protein primary structure....
17) Consider the following experimental methods that are commonly used in biochemistry: A) dynamic light scattering. B) polycrylamide gel electrophoresis (PAGE) with SDS present. C) polycrylamide gel electrophoresis (PAGE) without SDS present. D) surface plasmon resonance (SPR) E) differential scanning fluorimetry (DSF) F) analytical ultracentrifugation (equilibrium type) G) gel filtration chromatography (a) Which three of the methods are best for providing an estimate of the molecular weight of a protein in solution, in its native (non-denatured) form? (3 pts) Write...
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