Questions:

1. β-sheets found in a protein can be considered an example of:
  1. Primary structure
  2. Secondary structure
  3. Tertiary structure
  4. Quaternary structure
2. Which of the following statements best describes the tertiary structure of a protein?
  1. The 3-D conformation of a multisubunit protein, compose of a number of subunits joined by noncovalent interactions
  2. Local regions of polypeptide chains that have a regular conformation, which is stabilized by hydrogen bonds
  3. The total 3-D conformation of an entire polypeptide chain including a-helices, b-sheets and any other loops or bends.
  4. The linear sequence of amino acids in the polypeptide chain
  5. Certain types of conformational domains, which are composed of an assortment of α and β structures
3. All of the following are types of secondary structures EXCEPT
  1. α-helix
  2. β-sheet
  3. Bend or turn
  4. domain
4. R-groups in an α-helix:
  1. Extend outward from the central axis to avoid interfering sterically with each other
  2. Extend inward from the central axis
  3. Have to be close together to stabilize the helix
  4. Form the anti-parallel β-sheets
  5. Are hydrogen bonded to peptide bonds four amino acids away in th chain
5. All of the following statements regarding the R-groups in an α-helix are true EXCEPT:
  1. Runs of negative R-groups will disrupt the helix
  2. Runs of positive R-groups will stabilize the helix
  3. The R groups all protrude out from the central axis
  4. Runs of bulky R-groups will disrupt the helix because of steric hindrance
  5. Proline will destabilize the helix
6. A β-sheet consisting of β-strands connected laterally. Which of the following is TRUE of anti-parallel β-sheets?
  1. The N-termini of successive strands are oriented in the same direction
  2. The N-termini of successive strands are adjacent to one another
  3. Successive β strands alternate directions so that the N-terminus of one strand is adjacent to the C-terminus of the next
  4. Hydrophobic residues are located on both sides of the sheet
  5. The strands form hydrogen bonds with with loops or turns
7. All of the following statements regarding β-sheets are true EXCEPT?
  1. β-sheets are formed between 2 linear regions of polypeptide chains
  2. It is possible for one side of a b-sheet to be hydrophobic while the other side is hydrophilic
  3. Anti-parallel b-sheets are formed when the amino terminal to carboxy terminal directions of the two strands match
  4. Anti-parallel chains are often the same chain doubled back upon its self
  5. The two strands of a β-sheet are stabilized by hydrogen bonds
8. Which of the following is NOT a non-repetitive secondary structure?
  1. Bend
  2. Turn
  3. Loop
  4. Domain
9. Nonregular, nonrepetitive secondary structures
  1. Include α-helices and β-sheets
  2. Are bends, loops, and turns that do not have a repeating element
  3. Are beta-strands
  4. Are Beta-sheets
  5. Include beta-sheets
10. Motifs are supersecondary structures. Any motif can be defined by describing:
  1. The first 50 to 100 amino acids in the primary structure
  2. Any secondary structure and the turn at its C-terminus
  3. Any secondary structure and the loop at its N-terminus
  4. Any two secondary structures in the protein
  5. A group of secondary structures and their relationship to one another
11. A motif is best described as?
  1. Specific combinations of secondary structures that occur in a number of types of proteins
  2. Combinations of secondary structures that occur in only one enzyme from different species
  3. A specific primary sequence that occur in a number of types of proteins
  4. A structural domain
  5. A section of protein structure sufficient to perform a particular physical or chemical task
12. Which of the following is NOT true of structural domains?
  1. They usually contain a number of loops, turns or bends in addition to other secondary structures
  2. They usually contain of one or more secondary structural motifs
  3. They are usually about 25 or 300 amino acids in length
  4. They can maintain their conformation without the rest of the protein
  5. All the amino acids in the protein must be a part of the structural domains in the protein
13. A structural domain is best described as?
  1. A monomeric subunit in a quaternary protein
  2. Combinations of unstable secondary structures that occur in a number of types of proteins
  3. Loops that contain residues beyond the minimum number necessary to connect adjacent regions of secondary structure
  4. A series of secondary structures whose only common feature is that they form a turn, bend or loop
  5. A section of protein structure sufficient to perform a particular physical or chemical task
14. Proteins in a fold family usually share all of the following EXCEPT:
  1. Usually have a similar function
  2. Contain the same secondary structures
  3. Share a probable common evolutionary origin
  4. Have one or more domains
  5. Must contain only beta-strands or α-helix
15. Folds are relatively large patterns of 3-dimentional structures that have been recognized in domain(s) of one or more proteins. All of the following statements about folds are true, EXCEPT?
  1. It is believed that there are only a few thousand folds for all the proteins that ever existed
  2. Protein folds form because of the thermodynamic stability to the secondary structure arrangements
  3. Members of a fold have a similar arrangement of secondary structure in the domain
  4. Members of a fold have the same type of secondary structures
  5. Proteins often belong to more than one fold because it is very easy for an alpha-helix to become a beta-sheet
16. Folds are relatively large patterns of 3-dimentional structures that have been recognized in domain(s) of one or more proteins. All of the following statements about folds are true, EXCEPT?
  1. Members of a fold may have only beta strands
  2. Members of a fold may have only alpha-helices
  3. Members of a fold my contain a mixture of alpha helices and beta strands
  4. Members of a fold may contain only 7 beta strands
  5. Members of a fold are clearly related to one another by evolution
17.  If we say that two proteins are homologous, we are saying that they
  1. Probably derived from different ancestral genes
  2. Their tertiary structures would look dissimilar
  3. They probably have the same number and types of secondary structures oriented in the same way in space
  4. Their primary sequences would be 99% similar
  5. They have the different functions
18. Actin, heat shock protein 70 and hexokinase are homologous because:
  1. Their primary structures are very similar
  2. There is a structural correspondence between the three fold families that implies a common ancestral gene
  3. They all have the same primary structure
  4. Their evolution depended upon different genes and was not related
  5. They are only found in mammalian species
19. Which of the following amino acids is most likely to be found in the interior of a typical globular protein?
  1. Leucine
  2. Glutamate
  3. Threonine
  4. Lysine
  5. Serine
20. Which of the following statements is true with respect to the amino acids in a globular protein?
  1. Most of the hydrophobic amino acids are found in the center of globular proteins
  2. Most of the hydrophobic amino acids are found on the surface of globular proteins
  3. Most of the hydrophilic amino acids are found in the center of globular proteins
  4. Most of the charged amino acids are found in the center of globular proteins
  5. Glycine, valine, leucine, and isoleucine would normally be found on the surface
21. Third Edition only! The LDH molecule always contains 4 polypeptide subunits; each subunit can be either an H (heart) or an M (muscle) subunit. How many isozymes are possible?
  1. 3 isozymes
  2. 1 isozyme
  3. 2 isozymes
  4. 5 isozymes
  5. 4 isozymes
22. Third Edition only! The LDH molecule always contains 4 polypeptide subunits, which of the following best describes the isozymes of the LDH molecule?
  1. 2-homodimers and 2-heterotetramers
  2. 3-homotetramers and 2-heterotetramers
  3. 2-homotetramers and 3-heterotetramers
  4. 2-homodimers and 3-heterotetramers
  5. 2-homodimers and heterodimers
23. Third Edition only! Which of the following terms best describes the quaternary structure of the LDH molecule?
  1. Tetramer
  2. Monomer
  3. Oligomer
  4. Dimer
  5. Trimer
24. All of the following may be responsible for the formation and maintenance a protein's tertiary and quaternary protein structure. However, one of them is sometimes not present or forms only after the formation of the tertiary or quaternary structure and is important in stabilizing the structure?
  1. Hydrophobic interactions
  2. Disulfide bonds
  3. Hydrogen bonding
  4. Salt bridges
25. Which of the following best describes the forces that cause the monomer units of a quaternary structure to come together properly?
  1. Hydrophobic, electrostatic and covalent bonds
  2. Hydrophobic, electrostatic and hydrogen bonds
  3. Hydrophobic, electrostatic and disulfide bonds
  4. Electrostatic and hydrogen bonds only
  5. Only hydrogen bonds
26. The association constant, Ka, for a binding site on a protein is equal to?
  1. [Ligand]/[protein] [ligand-protein complex]
  2. [Ligand]/[ligand-protein complex]
  3. [Ligand-protein complex]/[ligand] [protein]
  4. [Ligand-protein complex]/[protein]
27. Knowing the Ka (association constant) or the Kd (dissociation constant) for a ligand-protein complex would be most useful for:
  1. Determining if the ligand is a weak acid
  2. Determining the concentration of ligand in solution
  3. Determining the affinity of different drugs for a receptor
  4. Determining the concentration of protein in solution
  5. Determining the pI of the protein
28. Similarities between hemoglobin and myoglobin include:
  1. They are located in the red blood cell
  2. They are both tetramers
  3. The heme of both hemoglobin and myoglobin is permanently oxidized as it binds oxygen
  4. Fe+2 of myoglobin and hemoglobin has eight coordination bonds, four of which are occupied by the nitrogen atoms of the porphyrin ring and the rest by histidine residues
  5. Heme of both hemoglobin and myoglobin is a prosthetic group
29. Which of the following statements accurately describe the hemoglobin molecule?
  1. The tertiary structure consists of eight beta-strands connected by α-helices (known as the globin fold)
  2. Hemoglobin is a tetramer composed of two different types of globin subunits, each of which has an O2 binding site
  3. Hemoglobin is a globular protein composed of a single polypeptide chain that has one O2 binding site
  4. The tetrameric structure of hemoglobin facilitates saturation with O2 as it travels through the capillary beds and release of O2 in the lungs
  5. The monomeric subunits are held together by disulfide bonds
30. Which statement best describes the myoglobin oxygen saturation curve?
  1. P50 for myoglobin is approximately 2.8 mm Hg
  2. P50 for myoglobin is approximately 26 mm Hg
  3. Myoglobin irreversibly binds a single molecule of oxygen so the dissociation curve is a straight line
  4. Cooperative binding of oxygen by the 4-subunits means that oxygen decreases the oxygen affinity of the remaining heme groups yielding a Sigmoidal-shaped curve
  5. The curve results because myoglobin can not bind oxygen as strongly as hemoglobin
31. Which of the following statements gives an accurate description of the O2 saturation curves for hemoglobin versus myoglobin?
  1. At lower levels of O2, myoglobin cannot bind oxygen as well as hemoglobin
  2. The O2 dissociation curve for hemoglobin is hyperbolic
  3. The O2 dissociation curve for myoglobin is sigmoidal
  4. Hemoglobin exhibits cooperative binding as the O2 concentration is raised
  5. Myoglobin exhibits cooperative binding as the O2 concentration is raised.
32. A ligand:
  1. Is a type of an amide linkage
  2. Can be a component of a holoprotein
  3. Can be a loosely bound prosthetic group
  4. Part of a tertiary protein stabilized by hydrogen bonding
  5. Is the group removed during the production of an enzyme from a proenzyme
33. Prosthetic groups of proteins are:
  1. Proteins with co-factors
  2. Protein portions of holoenzymes
  3. Tightly bound substances that don’t dissociate
  4. Derivatives of vitamins only
34. The oxygen dissociation curve for myoglobin has a hyperbolic shape that reflects the fact that:
  1. Myoglobin reversibly binds a single molecule of oxygen
  2. Myoglobin’s 4 subunits cooperate in binding oxygen
  3. The deoxy form of myoglobin is in the R-state
  4. Myoglobin has a lower oxygen affinity than hemoglobin
  5. Myoglobin has heme and hemoglobin does not
35. Which statement about immunoglobulin (Igs) is FALSE?
  1. They are peptides
  2. Each heavy chain is linked to a light chain
  3. The antigen binding domains have a non-variable (constant) amino acid sequence
  4. Each immunoglobulin contains 2 heavy chains
  5. Heavy chains are bound to each other by disulfide bonds
36. Which of the following descriptions of immunoglobulins is inaccurate?
  1. Both light and heavy chains of an immunoglobulin contain domains (regions) termed variable and constant
  2. The variable regions of the light and heavy chains (VL and VH) interact to produce a single antigen-binding site
  3. The constant domains are specific for the antigen that is bound; while the variable domains are the same for all antibody molecules regardless of class
  4. Each population of B-Cells produces an antibody with a different amino acid composition in the variable region that is complementary to the structure of the antigen eliciting the response
  5. The hinge region of an immunoglobulin allows flexibility when the molecule binds antigen
37. The tertiary conformation of a protein is determined by?
  1. The primary sequence
  2. Contact regions between the subunits of globular proteins
  3. The protein’s motifs
  4. Non-regular regions called coils
  5. The presence and numbers of disulfide bonds within the protein
38. Which of the following statements about protein denaturation is correct?
  1. Denaturation is always reversible
  2. Denaturation agents include detergents and heavy metals
  3. Proteins are pH and temperature resistant
  4. Denaturation only occurs through enzymatic modification of proteins
  5. Denaturation does not change the tertiary structure
39. Which of the following events are capable of denaturing a protein?
  1. Nonenzymatic glycosylation or oxidation
  2. Changes in temperature
  3. Solvents that disrupt ionic, hydrogen and hydrophobic bonds
  4. Contact with hydrophobic molecules such as long chain fatty acids
  5. All of the above
40. Prions are infectious proteins that:
  1. Are encoded by viruses
  2. Cleave DNA at specific sites
  3. Cleave proteins to cause their altered functionality
  4. Can catalyze an alternative folded state of a protein
  5. Protect disulfide bonds from being oxidized by reducing agents
41. All of the following statements regarding Prions are true, EXCEPT?
  1. The word prion stands for proteinaceous infectious agent
  2. Prion diseases can be acquired through infection, or from sporadic or inherited mutations
  3. Mad cow disease is an example of a prion disease that is acquired through infection
  4. Prion proteins are believed to cause a neurodegenerative disease by acting as a template to misfold other cellular prion proteins into a form that cannot be degraded
  5. Creutzfeldt-Jakob disease is an example of a prion disease that is transmitted by nucleic acid
42. All of the following occur as prions cause dementia EXCEPT?
  1. Normal proteins are converted into abnormal proteins
  2. Prions catalyze the production of more prions
  3. Misfolded proteins precipitated into aggregates that do not undergo proteolytic degradation
  4. A portion of alpha-helical and coil structure is refolded into beta-sheet
  5. PrPSC is converted into PrPC
43. All of the following lead to sickle cell crises EXCEPT
  1. The substitution of hydrophobic valine for glutamate in b-globin chains
  2. Low oxygen pressure in blood
  3. Increase production of deoxygenated polymers
  4. Increased deformability and stability of red blood cells
  5. Occlusion of small vessels in various tissues
44. The vasoocclusive crises experienced by an individual with Sickle cell disease:
  1. Is caused by hemoglobin molecules with the wrong quaternary structure
  2. Results from polymerization of HbS molecules into long fibers that distort the shape of the RBCs
  3. Will most likely occur in areas of lower O2 concentration such as venous capillary beds
  4. Results from the substitution of a hydrophobic valine for a glutamate in the B chains
  5. All of the above are factors that contribute to vasoocclusive crises in patients with Sickle cell disease
45. Which of the following cardiac tests has a very high negative predictive value within a 2 to 6 hour period following the onset of symptoms?  That is, this test will not tell you that your patient did have a heart attack but it is good at telling you that your patient did not have a heart attack.
  1. Myoglobin
  2. Creatine kinase, muscle-brain fraction (CK-MB)
  3. Troponin-I
  4. LDH
  5. AST
46. Which of the following statements correctly identifies three proteins that appear in the blood as a result of an occluded coronary artery that led to a myocardial infarction (MI)?
  1. Myoglobin, Troponin-T, and Creatine phosphokinase-MB
  2. Creatine phosphokinase-BB, Troponin-C, and Myoglobin
  3. Myoglobin, Bilirubin, and Troponin-C
  4. Troponin-I, Aspartate Amino Transferase, and Alkaline Phosphatase
  5. Aspartate Amino Transferase, Amylase and Troponin-C
47. All of the following statements are true regarding Amyloidosis/AL EXCEPT?
  1. Extracellular depositions of insoluble fibrillar proteins into organs and tissues
  2. AL is one type of amyloidosis characterized by deposition of amyloid fibers derived from constant regions of immunoglobulin heavy chains
  3. Multiple myeloma is an example of a disease entity in this category
  4. Serum protein electrophoresis may reveal an M-component, a sharp peak in the gamma-globulin fraction
  5. The amyloid fiber is composed of repeated beta-sheets aligned perpendicular to the long axis of the fiber
48. Minor hemoglobins play an essential role in understanding disease progression. Which of the following statement is TRUE of hemoglobin A1C?
  1. Results from non-enzymatic glycosylation
  2. Amount is Inversely related to plasma concentration of a particular hexose
  3. Diabetic patients have decreased amounts of HbA1C
  4. Glucose residues attach predominately to the amid nitrogen groups of the C-terminal glycine of the β-chain
  5. A low HbA1C would indicate one has a history of high blood glucose
49. Glycosylation is a nonenzymatic reaction that occurs with a rate directly proportionate to the concentration of glucose in the blood. As a percent of total HbA, what is the normal range of HbA1C ?
  1. 300 - 500%
  2. 10-30%
  3. 80-100%.
  4. 6-7%
  5. 0.01-0.5%
50. Concerning the binding of hemoglobin to O2, all of the following are true, EXCEPT?
  1. Hemoglobin may only bind 0, 1, or 4 molecules of O2
  2. Hemoglobin exists in two alternate conformations
  3. The T (tense) state (conformation) has a low affinity for O2
  4. The R (relaxed) state (conformation) has a higher affinity for O2
  5. Breaking the salt bridges between the subunits is an energy requiring process so the binding rate for the first oxygen is low
51. Forth Edition only! All of the following are true for the beta-adrenergic receptor, EXCEPT?
  1. It binds to epinephrine
  2. It has a ligand binding domain
  3. It contains seven hydrophilic beta-structures that span the membrane
  4. Some of the extracellular loops have carbohydrates attached
  5. The conformation of the binding site changes when adrenalin is bound
52. Forth Edition only! All of the following are true when adrenalin binds to the beta-adrenergic receptor, EXCEPT?
  1. The conformation of the ligand binding domain changes.
  2. The conformation of the transmembrane portion (domain) changes.
  3. The intracellular portion of the receptor changes conformation.
  4. The intracellular portion of the receptor binding binds to G-protein.
  5. The intracellular portion of the receptor forms a covalent bond with G-protein.
53. Forth Edition only! What is the general name for the class of proteins that help other proteins fold into their native tertiary conformation?
  1. Heat shock proteins
  2. Bence-Jones proteins
  3. Prions
  4. Gamma globulins
  5. Homologs

Answers:

1. Answer: B. Chapter 7, Objective 1: Understand the meaning of primary, secondary, tertiary, and quaternary structure and be able to discern the difference. Back to question 1.
2. Answer: C. Chapter 7, Objective 1: Understand the meaning of primary, secondary, tertiary, and quaternary structure and be able to discern the difference. Back to question 2.
3. Answer: D. Chapter 7, Objective 2: Be able to recognize and discern between the three types of secondary structure discussed in class! Back to question 3.
4. Answer: A. Chapter 7, Objective 3: What is the location of the R-groups in an alpha helix? Can an alpha helix be formed from any primary sequence of amino acids? Back to question 4.
5. Answer: B. Chapter 7, Objective 3: What is the location of the R-groups in an alpha helix? Can an alpha helix be formed from any primary sequence of amino acids? Back to question 5.
6. Answer: C. Chapter 7, Objective 4 and 5: What is the difference between parallel and anti-parallel b-sheets? How do the R-groups protrude from the sheets? Back to question 6.
7. Answer: C. Chapter 7, Objective 4: What is the difference between parallel and anti-parallel b-sheets? How do the R-groups protrude from the sheets? Back to question 7.
8. Answer: D. Chapter 7, Objective 5: What are the three names for nonregular, nonrepetitive secondary structures? Back to question 8.
9. Answer: B. Chapter 7, Objective 5: What are the three names for nonregular, nonrepetitive secondary structures? Back to question 9.
10. Answer: E. Chapter 7, Objective 6: What is a motif? Back to question 10.
11. Answer: A. Chapter 7, Objective 6: What is a motif? Back to question 11.
12. Answer: E. Chapter 7, Objective 7: What is a structural domain? Back to question 12.
13. Answer: E. Chapter 7, Objective 7: What is a structural domain? Back to question 13.
14. Answer: E. Chapter 7, Objective 8: What is a fold (fold structure or protein fold)? What is a fold family? Back to question 14.
15. Answer: E. Chapter 7, Objective 8: What is a fold (fold structure or protein fold)? What is a fold family? Back to question 15.
16. Answer: E. Chapter 7, Objective 8: What is a fold (fold structure or protein fold)? What is a fold family? Back to question 16.
17. Answer: C. Chapter 7, Objective 9: When we say that actin, heat shock protein 70, and hexokinase are homologous, what are we implying? Back to question 17.
18. Answer: B. Chapter 7, Objective 9: When we say that actin, heat shock protein 70, and hexokinase are homologous, what are we implying? Back to question 18.
19. Answer: A. Chapter 7, Objective 10: Where would you most likely find the nonpolar, polar and charged amino acids in a globular protein? Back to question 19.
20. Answer: A. Chapter 7, Objectives 10: Where would you most likely find the nonpolar, polar and charged amino acids in a globular protein? Back to question 20.
21. Answer: D. Chapter 7, Objectives 11: The LDH molecule always contains 4 polypeptide subunits and each subunit can be either an H (heart) or an M (muscle) subunit. How many isozymes are possible? Describe the molecule in terms of the number of mers and homo or hetero. Back to question 21.
22. Answer: C. Chapter 7, Objective 11: The LDH molecule always contains 4 polypeptide subunits and each subunit can be either an H (heart) or an M (muscle) subunit. How many isozymes are possible? Describe the molecule in terms of the number of mers and homo or hetero. Back to question 22.
23. Answer: A. Chapter 7, Objective 11: The LDH molecule always contains 4 polypeptide subunits and each subunit can be either an H (heart) or an M (muscle) subunit. How many isozymes are possible? Describe the molecule in terms of the number of mers and homo or hetero. Back to question 23.
24. Answer: B. Chapter 7, Objective 12: What are the forces that hold the monomer units of a quaternary structure together? Back to question 24.
25. Answer: B. Chapter 7, Objective 12: What are the forces that hold the monomer units of a quaternary structure together? Back to question 25.
26. Answer: C. Chapter 7, Objective 13: For a ligand-protein complex that dissociates into a ligand and protein, be able to state the dissociation constant and the association constant. Back to question 26.
27. Answer: C. Chapter 7, Objective 13: For a ligand-protein complex that dissociates into a ligand and protein, be able to state the dissociation constant and the association constant. Back to question 27.
28. Answer: E. Chapter 7, Objective 14: Using the terms ferrous iron, heme, hydrophobic pocket, histidine, alpha-helix, alpha-turns, salt bonds, hydrophobic interactions, hydrogen bonds, oxygen, and subunits, describe the myoglobin and hemoglobin molecule. Back to question 28.
29. Answer: B.  Chapter 7, Objective 14: Using the terms ferrous iron, heme, hydrophobic pocket, histidine, alpha-helix, alpha-turns, salt bonds, hydrophobic interactions, hydrogen bonds, oxygen, and subunits, describe the myoglobin and hemoglobin molecule. Back to question 29.
30. Answer: A.  Chapter 7, Objective 15: Be able to draw an oxygen dissociation curve for hemoglobin and myoglobin. Back to question 30.
31. Answer: D.  Chapter 7, Objective 15: Be able to draw an oxygen dissociation curve for hemoglobin and myoglobin. Back to question 31.
32. Answer: B. Chapter 7, Objective 16: What is a ligand? Back to question 32.
33. Answer: C. Chapter 7, Objective 17: What is a prosthetic group? Back to question 33.
34. Answer: A. Chapter 7, Objective 18: Be able to explain why the oxygen saturation curve for hemoglobin is sigmoidal while the curve for myoglobin is a rectangular hyperbola. Include the terms subunits, O2, Fe2+, conformation, salt bridges, T-state, R-state. Back to question 34.
35. Answer: C. Chapter 7, Objective 19: Be able to describe the structure of IgG in terms of the number of chains, the number and types of domains, and the forces that hold the chains together. Which part binds to an antigen and why is it specific? What fold family do the domains belong to. Back to question 35.
36. Answer: C. Chapter 7, Objective 19: Be able to describe the structure of IgG in terms of the number of chains, the number and types of domains, and the forces that hold the chains together. Which part binds to an antigen and why is it specific? What fold family do the domains belong to. Back to question 36.
37. Answer: A Chapter 7, Objective 20: What determines the tertiary conformation of a protein? Back to question 37.
38. Answer: B. Chapter 7, Objective 21: What is denaturation? Name a few ways that proteins are denatured in humans. Back to question 38.
39. Answer: E Chapter 7, Objective 21: What is denaturation? Name a few ways that proteins are denatured in humans. Back to question 39.
40. Answer: D. Chapter 7, Objective 22: What is a prion? Back to question 40.
41. Answer: E. Chapter 7, Objective 22: What is a prion? Back to question 41.
42. Answer: E. Chapter 7, Objective 23: Explain how a prion can cause dementia and death. Include the terms PrPc, PrPsc, template, activation energy, cascade, amyloid protein, and proteolytic degradation. Back to question 42.
43. Answer: D. Chapter 7, Objective 24: Concerning Will Sichel: In biochemical terms, explain the development of pain during a sickle cell crises. Include the specific mutation, oxygen pressure, and protein conformation in your answer. Back to question 43.
44. Answer: E. Chapter 7, Objective 24: Concerning Will Sichel: In biochemical terms, explain the development of pain during a sickle cell crises. Include the specific mutation, oxygen pressure, and protein conformation in your answer. Back to question 44.
45. Answer: A. Chapter 7, Objective 25: Concerning Anne Jeina: What are the three different proteins that appear in the blood following the beginning of a myocardial infarction? What are their normal cell functions? How soon can they be detected? How specific are they? Back to question 45.
46. Answer: A. Chapter 7, Objective 25: Concerning Anne Jeina: What are the three different proteins that appear in the blood following the beginning of a myocardial infarction? What are their normal cell functions? How soon can they be detected? How specific are they? Back to question 46.
47. Answer: B. Chapter 7, Objective 26: Concerning Amy Lloyd: What is an amyloid protein? What are the monomer units of the polymer in amyloidosis/AL? What secondary structure is found in amyloid fibers? What is an M-protein and why is it detected as a sharp peak upon serum protein electrophoresis? Back to question 47.
48. Answer: A. Chapter 7, Objective 27: Concerning Di Abietes, What is HbA1c? How is it made and what does it measure? Back to question 48.
49. Answer: D. Chapter 7, Objective 27: Concerning Di Abietes, What is HbA1c? How is it made and what does it measure? Back to question 49.
50. Answer: A. Chapter 7, Objective 18. Be able to explain why the oxygen saturation curve for hemoglobin is sigmoidal while the curve for myoglobin is a rectangular hyperbola. Include the terms subunits, O2, Fe2+, conformation, salt bridges, T-state, R-state Back to question 50.
50. Answer: A. Chapter 7, Objective 18. Be able to explain why the oxygen saturation curve for hemoglobin is sigmoidal while the curve for myoglobin is a rectangular hyperbola. Include the terms subunits, O2, Fe2+, conformation, salt bridges, T-state, R-state Back to question 50.
51. Answer: C. Chapter 7, Objective 11: In the beta-adrenergic receptor, where do you find the bound carbohydrate, the ligand binding site, the 7 alpha-helical domains, and the G-protein binding site? Why is part of the polypeptide chain in the membrane? When the hormone binds, does the receptor change its conformation? Back to question 51.
52. Answer: E. Chapter 7, Objective 11: In the beta-adrenergic receptor, where do you find the bound carbohydrate, the ligand binding site, the 7 alpha-helical domains, and the G-protein binding site? Why is part of the polypeptide chain in the membrane? When the hormone binds, does the receptor change its conformation? Back to question 52.
53. Answer: a. Chapter 7, Objective 20: What is the general name for the class of proteins that help other proteins fold into their native tertiary conformation? Back to question 53.