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Biochem-Samplex Le

The document contains a 21 question biochemistry exam covering topics like: 1) Properties of water and its role in protein structure. 2) Types of chemical bonds like covalent and hydrogen bonds. 3) Diseases resulting from nutrient deficiencies like scurvy. 4) Key aspects of hemoglobin function and genetic disorders that affect it. 5) Characteristics of protein structure like secondary structure, folding and interactions between residues.

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Carlos Niño
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0% found this document useful (0 votes)
258 views

Biochem-Samplex Le

The document contains a 21 question biochemistry exam covering topics like: 1) Properties of water and its role in protein structure. 2) Types of chemical bonds like covalent and hydrogen bonds. 3) Diseases resulting from nutrient deficiencies like scurvy. 4) Key aspects of hemoglobin function and genetic disorders that affect it. 5) Characteristics of protein structure like secondary structure, folding and interactions between residues.

Uploaded by

Carlos Niño
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Download as DOCX, PDF, TXT or read online on Scribd
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BIOCHEM-LONG EXAMS

SAMPLEX

1. The propensity of water molecules to form hydrogen bonds with one another is
the primary factor responsible for all of the following properties of water EXCEPT:
A.Its atypically high boiling point.
B.Its high heat of vaporization.
C.Its high surface tension.
D.Its ability to dissolve hydrocarbons.
E.Its expansion upon freezing.

2. Which one of the following types of bonds is


covalent?
(A) Hydrophobic
(B) Hydrogen
(C) Disulfide
(D) Electrostatic
(E) Van der Waals

3. An environmentalist attempted to live in a


desolate forest for 6 months, but had to cut his
experiment short when he began to suffer from
bleeding gums, some teeth falling out, and red
spots on the thighs and legs. This individual is
suffering from an inability to properly synthesize
which one of the following proteins?
(A) Myoglobin
(B) Hemoglobin
(C) Collagen
(D) Insulin
(E) Fibrillin

4. Which one of the following is the amino


acid in hemoglobin that accepts H+ and allows
hemoglobin to act as a buffer to acids?
(A) Alanine
(B) Histidine
(C) Serine
(D) Threonine
(E) Aspartate
5. Select the one of the following statements that is NOT CORRECT.
A.The side-chains of the amino acids cysteine and methionine absorb light at 280
nm
B.Glycine is often present in regions where a polypeptide forms a sharp bend,
reversing the direction of a polypeptide.
C.Polypeptides are named as derivatives of the C-terminal aminoacyl residue.
D.The C, N, O, and H atoms of a peptide bond are coplanar.
E.A linear pentapeptide contains four peptide bonds.

6. Select the one of the following statements that is NOT CORRECT.


A.Buffers of human tissue include bicarbonate, proteins, and orthophosphate.
B.A weak acid or a weak base exhibits its greatest buffering capacity when the
pH is equal to its pKa plus or minus one pH unit.
C.The isoelectric pH (pI) of lysine can be calculated using the formula (pK2+
pK3)/2.
D.The mobility of a monofunctional weak acid in a direct current electrical field
reaches its maximum when the pH of its surrounding environment is equal to its
pKa.
E.For simplicity, the strengths of weak bases are generally expressed as the pKa
of their conjugate acids

7. Select the one of the following statements that is NOT CORRECT.


A.A major objective of proteomics is to identify all of the proteins present in a cell
under different conditions as well as their states of modification.
B.Mass spectrometry has largely replaced the Edman method for sequencing of
peptides and proteins.
C.Sanger reagent was an improvement on Edman’s because the former
generates a new amino terminus, allowing several consecutive cycles of
sequencing to take place.
D.Since mass is a universal property of all atoms and molecules, mass
spectrometry is ideally suited to the detection of posttranslational modifications in
proteins.
E.Time-of-flight mass spectrometers take advantage of the relationship F = ma

8. Unknownst to its owners, a cow recently


sacrificed for meat production had mad cow
disease. The precipitating event in the cow’s
brain that led to this disease is which one of the
following?
(A) Altered gene expression
(B) Infection of the brain with a virus
(C) Proteolytic cleavage of an existing brain
protein
(D) An altered secondary and tertiary structures
for an existing brain protein
(E) Loss of the nuclear membrane

9. A family has been using an additional propane


heater in their enclosed apartment during
the winter months. One morning, a family
member is difficult to awake, and when awake,
complains of a splitting headache and being
very tired. His mucous membranes are also a
cherry red color. These symptoms are the result
of which one of the following?
(A) Increased oxygen delivery to
the tissues
(B) Decreased oxygen delivery to
the tissues
(C) Increased blood flow to the brain
(D) Decreased blood flow to the brain
(E) Decreased oxygen affinity to hemoglobin

10. Select the one of the following statements that is NOT CORRECT.
A.Protein folding is assisted by intervention of specialized auxiliary proteins
called chaperones.
B.Protein folding tends to be modular, with areas of local secondary structure
forming first, then coalescing into a molten globule.
C.Protein folding is driven first and foremost by the thermodynamics of the water
molecules surrounding the nascent polypeptide.
D.The formation of S-S bonds in a mature protein is facilitated by the enzyme
protein disulfide isomerase.
E.Only a few unusual proteins, such as collagen, require posttranslational
processing by partial proteolysis to attain their mature conformation

11. Select the one of the following statements that is NOT CORRECT.
A.Posttranslational modifications of proteins can affect both their function and
their metabolic fate.
B.The native conformational state generally is that which is thermodynamically
favored.
C.The complex three-dimensional structures of most proteins are formed and
stabilized by the cumulative effects of a large number of weak interactions.
D.Research scientists employ gene arrays for the high-throughput detection of
the presence and expression level of proteins.
E.Examples of weak interactions that stabilize protein folding include hydrogen
bonds, salt bridges, and van der Waals forces.

12. Select the one of the following statements that is NOT CORRECT.
A.The descriptor a2β2γ3 denotes a protein with seven subunits of three different
types.
B.Loops are extended regions that connect adjacent regions of secondary
structure.
C.More than half of the residues in a typical protein reside in either a helices or β
sheets.
D.Most β sheets have a right-handed twist.
E.Prions are viruses that cause protein-folding diseases that attack the brain.

13. Select the one of the following statements that is NOT CORRECT:
A.The Bohr effect refers to the release of protons that occurs when oxygen binds
to deoxyhemoglobin.
B.Shortly after birth of a human infant, synthesis of the α-chain undergoes rapid
induction until it comprises 50% of the hemoglobin tetramer.
C.The β-chain of fetal hemoglobin is present throughout gestation.
D.The term thalassemia refers to any genetic defect that results in partial or total
absence of the α- or β-chains of hemoglobin.
E.The taut conformation of hemoglobin is stabilized by several salt bridges that
form between the subunits

14. Select the one of the following statements that is NOT CORRECT:
A.Steric hindrance by histidine E7 plays a critical role in weakening the affinity of
hemoglobin for carbon monoxide (CO).
B.Carbonic anhydrase plays a critical role in respiration by virtue of its capacity to
break down 2,3-bisphosphoglycerate in the lungs.
C.Hemoglobin S is distinguished by a genetic mutation that substitutes Glu6 on
the β subunit with Val, creating a sticky patch on its surface.
D.Oxidation of the heme iron from the +2 to the +3 state abolishes the ability of
hemoglobin to bind oxygen.
E.The functional differences between hemoglobin and myoglobin reflect, to a
large degree, differences in their quaternary structure.

15. The simplest amino acid that shows no optical activty:


a. Alanine
b. Lysine
c. Phenylalanine
d. Glycine

16. In a polypeptide at physiologic pH, hydrogen bonding may occur between which of
the following?
A. The side chains of a leucine residue and a lysine residue
B. The side chains of an aspartyl residue and a gluta-myl residue
C. The terminal alpha-amino group and the terminal alpha-carboxyl group
D. The amide group in the peptide bond and an aspartyl side chain
E. The –SH groups of two cysteine residues

17. Which of the following shows the linear sequence of atoms joined by covalent bonds
in a peptide backbone?
A. –N–C–C–N–C–C–N–C–C
B. –N–C–O–N–C–O–N–C–O–
C. –N–C–C–O–N–C–C–O–N–C–C–O–
D. –N–H–C–C–N–H–C–C–N–H–C–C–
E. –N–H–C–O–H–N–H–C–O–H–N–H–C–C–

18. Protein kinases phosphorylate proteins only at certain hydroxyl groups on amino
acid side chains. Which of the following groups of amino acids all contain side-chain
hydroxyl groups?
A. Aspartate, glutamate, and serine
B. Serine, threonine, and tyrosine
C. Threonine, phenylalanine, and arginine
D. Lysine, arginine, and proline
E. Alanine, asparagine, and serine

19. Which of the following characterize -helix regions of proteins?


A. They all have the same primary structure.
B. They are formed principally by hydrogen bonds between a carbonyl oxygen
atom in one peptide bond and the amide hydrogen from a different pep-tide bond.
C. They are formed principally by hydrogen bonds between a carbonyl atom in
one peptide bond and the hydrogen atoms on the side chain of another amino acid
.D. They are formed by hydrogen bonding between two adjacent amino acids in
the primary sequence.
E. They require a high content of proline and glycine.

20. Which of the following is a characteristic of globular proteins?


A. Hydrophilic amino acids tend to be on the inside.
B. Hydrophobic amino acids tend to be on the outside.
C. Tertiary structure is formed by hydrophobic and electrostatic
interactions between amino acid side chains and by hydrogen bonds between
peptide bonds.
D. Secondary structures are formed principally by hydrophobic
interactions between amino acids.
E. Covalent disulfide bonds are necessary to hold the protein in a rigid
conformation.

21. A protein has one transmembrane domain composed entirely of -helical secondary
structure. Which of the following amino acids would you expect to find in the
transmembrane domain?
A. Proline
B. Glutamate
C. Lysine
D. Leucine
E. Arginine

22. Autopsies of patients with Alzheimer disease show pro-tein aggregates called
neurofibrillary tangles and neuritic plaques in various regions of the brain. These
plaques exhibit the characteristic staining of amyloid. Which of the following structural
features is the most likely charac-teristic of at least one protein in these plaques?
A. A high content of Beta-pleated sheet structure
B. A high content of alpha-helical structure
C. A high content of random coils
D. Disulfide bond cross-links between polypeptide chains
E. A low-energy native conformation

23. Enzyme containing organic molecules that are derived from vitamins and are
essential for activity
A. Holoenzyme
B. Apoenzyme
C. Coenzyme
D. Both A and C
E. None of the above

24. For non competitive inhibition Vmax is


A. Increased
B. Decreased
C. Unchanged
D. Increased then decreased
E. Decreased then increased

25. Which of the following describes competitive inhibitors


A. It decreased the number of free enzyme molecules available to bind substrate.
B. Can overcome by decreasing substrate
C. Vmax is constant, Km is increased
D. Both A and B
E. Both A and C

26. Which of the following is Michaelis-menten Equation:

A.

B.

C.

D. .

27. Which of the following statements is are unlikely of the enzyme:


A. Does not change the equilibrium constant of the reaction
B. Accelerates the free energy activation
C. Recovered unchanged after the completion of the reaction
D. None of the above

28. Serves as a precursor of epinephrine, norepinephrine and DOPA:


A. Tyrosine
B. Phenylalanine
C. Valine
D. Both A and B
E. Both B and C
29. An autosomal recessive disorder affecting branched-chain 2-keto acid
decarboxylase characterized with sweet odor.
A. Homocystinuria
B. Maple-syrup urine disease
C. Phenylketonuria
D. Histidinemia
E. None of the above

30. Absence of tyrosinase will cause:


A. Phenylketonuria
B. Maple-syrup Syndrome
C. Albinism
D. Homocytinuria
E. Histidinemia

31. All of the following are true causes of enzyme denaturation EXCEPT:
A. Change in pH
B. Change in Temperature
C. High Concentration of neutral polar compounds
D. Vigorous shaking and stirring of aqueous solutions
E. None of the above

32. Transmissible spongiform encephalopathy in sheep:


A. Creutzfeldt-Jacob Disease
B. Scrapie
C. Mad Cow Diseases
D. Scurvy
E. None of the above

33. Which of the following does not describe Van Der Waal’s Forces:
A. Weaker than hydrogen bonds, but extremely numerous.
B. Arises from attractions between transients dipole generated by the rapid
movement of electrons of all neutral atoms.
C. Facilitate the binding of charged molecules and ions to CHONs and Nucleic acids
D. strength of interactions varies with the distance, R, between interacting species.
E. Both A and B

34. Metabolic acidosis can be corrected by:


A. Hyperventilation
B. Increased renal excretion of H-
C. Hypoventilation
D. Decreased renal excretion of H-

35. Respiratory alkalosis compensatory mechanism:


A. Hyperventilation
B. Increased renal excretion of H-
C. Hypoventilation
D. Decreased renal excretion of H-

36. Which of the following is Henderson-Hasselbach Equation:

A.

B.

C.

D.
E. None of the above
37. The oxygen-myoglobin dissociation curve is?
A. Linear curve
B. Hyperbolic curve
C. Bell curve
D. None of the above

38. Hemoglobin is characterized as waxy inside and soapy outside because of:
A. Hydrophilic acid outside
B. Hydrophobic amino acid inside
C. Hydrophobic acid outside
D. Both A and B
E. Both B and C

39. 15 year old boy recurrent joint pains and anemia is noted to have abnormally
shaped red cells on a peripheral smear. Further hematologic studies indicate that the
abnormality is assoc. with altered surface properties of hemoglobin. He is likely
suffering from:
A. Alpha Thalassemia
B. Beta Thalassemia
C. Sickle cell Anemia
D. Iron deficiency anemia
E. None of the above

40. Thalassemia is associated with genetic defects of hemoglobin which includes:


A. Absence or ineffective synthesis of hemoglobin alpha or beta chain
B. Excessive synthesis of hemoglobin alpha or beta chain
C. Activation of all alpha and beta globin genes
D. Both A and B
E. Both B and C

41. A polypeptide with a net positive charge at physiologic pH (~7.4) most likely
contains amino acids with R groups of what type?
a. Acidic R group
b. Aromatic R group
c. Aliphatic R group
d. Basic R group

42. Which of the following properties of a protein is least likely to be affected by


changes in pH?
a. Tertiary
b. Primary
c. Secondary
d. Net charge
43. When amino acids are bonded into a single long chain, the resulting product is
considered to be a protein's....

A. Primary Structure
B. Secondary Structure
C. Tertiary Structure
D. Quaternary Structure

44. Proteins embedded in the cellular membrane are often used for many functions.
Which of these is not a function of membrane proteins.

a. Cell adhesion
b. Receptor site for hormone
c. Transport material
d. Cell identity or recognition
e. Cell nutrition
45. Which of the following is NOT true about Proteins?

a. They are insoluble in water due to their size & heavy molecular mass.
b. They are the building block of many mammalian tissues, such as muscle
or bone.
c. They are stored as a nutrient, since they yield more energy than lipids or
carbs.
d. They are useful in cells as both structural components & in chemical
reactions.

46. If a protein consists of several different polypeptides, each with a complex three-
dimensional shape, held together by chemical bonds, it is considered to have a fairly
complex ____________ structure.

A. Primary
B. Secondary
C. Tertiary
D. Quaternary

47. Which of the following statements is NOT true regarding the comparison of the alpha-helix
structure to the beta-sheet structure in proteins?

A. The peptide bond in each is planar and trans

B. All possible hydrogen bonds between the peptide carbonyl oxygen (C=O) and the amide
hydrogen (N-H) are formed in each

C. Each may occur in typical globular proteins

D. Each is an example of secondary structure

E. Each is stabilized by inter-chain hydrogen bonds

48. Which of the following describes the folding of soluble globular proteins?

A. Most hydrophobic amino acids are internal, away from solvent water

B. The energy of the system (protein + water) is at a maximum

C. None of the answers are true

D. Two of the answers are true


E. Most hydrophilic amino acid residues are protected from water

49. What portions of the amino acids in hemoglobin likely mediate the differences in the binding
and non-binding regions of hemoglobin?

A. Peptide bond

B. Amino termini

C. Carboxy termini

D. Alpha carbon

E. Side chains

50. Which of the following is the LEAST important force that promotes protein folding?

A. Dipole interactions

B. Metallic bonding

C. Van der Waals interactions

D. Covalent bonding

E. Hydrogen bonding

KEY:

1. D 2. C 3. C 4. B 5. A 6. D 7. C 8. B 9. B 10. E 11. D 12. E 13.


B 14. B 15. D 16. D 17. A 18. B 19. B 20. C 21. D 22. A 23.C
24. B 25.E 26. B 27. D 28. D 29.B 30. C. 31. E 32. B 33. C
34. A 35. D 36. A 37. B 38. D 39. C 40. A 41. D 42. B 43.A
44. E 45. C 46. D 47. E 48. E 49. E 50. E

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