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Chaperone proteins Select one: Target damaged proteins for degradation b. Contribute to protein folding c. Are...
1) Select all that apply. Globular proteins: a)are found in hair and wool. b)include myoglobin and...
1) Select all that apply. Globular proteins: a)are found in hair and wool. b)include myoglobin and collagen. c)are usually water soluble. d)aggregate in aqueous media. e)are often made of β-pleated sheet and α-helix sections wrapped into compact structures. 2) Select all that apply. The Bohr effect: a)depends on the atomic orbital structure of hydrogen. b)can be summarized as a reduction in the oxygen affinity of hemoglobin with decreasing pH. c)is explained by the protonation of key amino acids, including the...
The correct folding of proteins is necessary to maintain healthy cells and tissues. Unfolded proteins are...
The correct folding of proteins is necessary to maintain healthy cells and tissues. Unfolded proteins are responsible for such neurodegenerative disorders as Alzheimer's, Huntington's, and Creutzfeld-Jacob disease (the specific faulty protein is different for each disease). What is the ultimate fate of these disease causing, unfolded proteins? A. They form structured filaments, B. They form protein aggregates. C. They bind a different target protein. D. They are degraded.
Degradation of a protein can be activated by: select all that apply covalent modifications to the...
Degradation of a protein can be activated by: select all that apply covalent modifications to the target protein covalent modifications to a protein that interacts with the target protein covalent modifications to the E3 changes in gene expression for a protein that interacts with the E3
10. Protein folding, in most cases, is complex and inhibited by aggregation. Which of the following...
10. Protein folding, in most cases, is complex and inhibited by aggregation. Which of the following is false regarding protein folding? A. Chaperones of the heat shock classes do not promote folding, but rather inhibit aggregation. B. Enzymes promote the formation of proper disulfide linkages by eliminating improper folding. C. All proteins require the input of energy and the assistance of chaperones for folding. D. Secondary structures usually form first in folding.
For a protein such as ribonuclease, for the process of protein folding under native (non-denaturing) conditions,...
For a protein such as ribonuclease, for the process of protein folding under native (non-denaturing) conditions, Punfolded → Pfolded Select the appropriate description for each of the thermodynamic parameters (for the folding reaction as shown above, from left to right): What is the value of ∆G? What is the value of ∆Sconformational? The value of ∆S hydrophobic? The choices for each question A. positive, favorable for folding B. positive, unfavorable for folding C. negative, favorable for folding D. negative, unfavorable...
21. Which of the following would NOT change the structure and function of a protein A...
21. Which of the following would NOT change the structure and function of a protein A Methylation of a protein B. Lipid modification of a protein C Change in the length of the Poly A tail of the mRNA transcript encoding a protein D. Change in the position of reactive amino acids E. Proteolysis 22. Two peptides have almost the exact same primary structure, except that one has about 10 fewer amino acids at the amino-terminus (N-terminus) of the protein....
Which one of the following proteins is an extracellular protein? a. vinculin b. laminin c. dynamin...
Which one of the following proteins is an extracellular protein? a. vinculin b. laminin c. dynamin d. lamin e. tubulin The phenomenonon of rigor mortis occurs due to: a. Inactivation of the Ca++ pump b. Discontinuation of ATP production c. Inability of myosin to release actin d. All of the above e. Onlyaandc
In RNA interference studies, the double-stranded RNA Select one: a. disrupts the target DNA sequence b....
In RNA interference studies, the double-stranded RNA Select one: a. disrupts the target DNA sequence b. results in the destruction of the target mRNA c. destroys the target protein d. all of the above Hint: it's not D
Match the following: Integral (intrinsic) membrane proteins Transmembrane protein Porins C-- Lipid-linked proteins Peri...
Match the following: Integral (intrinsic) membrane proteins Transmembrane protein Porins C-- Lipid-linked proteins Peripheral (extrinsic) proteins 1. Channel-forming proteins found in the outer membranes of bacteria, with a beta-barrel motif. 2. Proteins that are associated with membranes, but can be dissociated by relatively mild procedures. 3. Proteins that completely span the membrane. 4. A general class of proteins that are tightly bound to membranes by hydrophobic interactions. 5. Membrane-associated proteins that have covalently-bonded lipids.
Which protein modification does NOT take place in the ER lumen? A. Polyubiquitylation &nbs
Which protein modification does NOT take place in the ER lumen? A. Polyubiquitylation B. N-linked glycosylation C. Cysteine bridge formation D. chaperone-mediated folding E. GPI anchoring 2. Which of these Eukaryotic proteins is least likely to exhibit an ER import sequence during translation? A. Glutathione B. CFTR C. Protein disulfide isomerase D. Acetylcholine receptor E. Na+-K+-ATPase 3. Which function is NOT attributed correctly to either smooth ER (SER) or rough ER (RER)?...
The correct folding of proteins is necessary to maintain healthy cells and tissues. Unfolded proteins are responsible for such neurodegenerative disorders as Alzheimer's, Huntington's, and Creutzfeld-Jacob disease (the specific faulty protein is different for each disease). What is the ultimate fate of these disease causing, unfolded proteins? A. They form structured filaments, B. They form protein aggregates. C. They bind a different target protein. D. They are degraded.
10. Protein folding, in most cases, is complex and inhibited by aggregation. Which of the following is false regarding protein folding? A. Chaperones of the heat shock classes do not promote folding, but rather inhibit aggregation. B. Enzymes promote the formation of proper disulfide linkages by eliminating improper folding. C. All proteins require the input of energy and the assistance of chaperones for folding. D. Secondary structures usually form first in folding.
21. Which of the following would NOT change the structure and function of a protein A Methylation of a protein B. Lipid modification of a protein C Change in the length of the Poly A tail of the mRNA transcript encoding a protein D. Change in the position of reactive amino acids E. Proteolysis 22. Two peptides have almost the exact same primary structure, except that one has about 10 fewer amino acids at the amino-terminus (N-terminus) of the protein....
Match the following: Integral (intrinsic) membrane proteins Transmembrane protein Porins C-- Lipid-linked proteins Peripheral (extrinsic) proteins 1. Channel-forming proteins found in the outer membranes of bacteria, with a beta-barrel motif. 2. Proteins that are associated with membranes, but can be dissociated by relatively mild procedures. 3. Proteins that completely span the membrane. 4. A general class of proteins that are tightly bound to membranes by hydrophobic interactions. 5. Membrane-associated proteins that have covalently-bonded lipids.
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